6zii: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
Line 3: Line 3:
<StructureSection load='6zii' size='340' side='right'caption='[[6zii]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='6zii' size='340' side='right'caption='[[6zii]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6zii]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZII FirstGlance]. <br>
<table><tr><td colspan='2'>[[6zii]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZII FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BFD:ASPARTATE+BERYLLIUM+TRIFLUORIDE'>BFD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rcsB, A2O69_13765, A3042_19525, A3104_15245, A3111_09650, A3122_12425, A3146_09020, A3R41_09960, A3S30_08650, A3T21_09515, A3T81_14325, A3U32_14885, A3V03_11040, A3V89_10805, A3W57_14915, A3W75_12230, A3W86_06130, A3X15_13890, A3X55_20780, A3Y76_07040, A3Z96_14340, A4J27_11660, A4N07_14810, A4O05_20855, A4O41_07785, A4R48_08340, A6D61_15370, A9C21_06135, A9R92_21345, A9T39_16135, A9U46_10475, A9U64_21675, A9U69_21545, AAA76_10930, AAB27_22280, AAB39_09270, AAB79_16325, AAC08_11475, AAC35_11250, AAC42_16960, AAC44_14685, AAC95_13155, AAC98_10995, AAK29_10400, AAP89_11275, AAQ24_16295, AB424_18490, ABO94_17915, ABP11_15160, ABP87_18790, ABQ69_20575, ADQ28_04890, ADQ45_05825, AE787_14130, AF480_10895, AF488_12145, AF489_17255, AF497_17465, AGC55_06475, AGM99_13695, AGQ32_04375, AH984_14180, AHN93_10200, AIC76_12470, AKH62_06605, AKH68_10310, AKI16_13295, AL144_14225, AL151_13230, AL166_17425, AL168_14180, AL170_15835, AL174_14280, AL184_16885, APP08_20700, APY91_13970, AQ530_14880, AQ536_13855, AS118_05400, AT354_14865, AU613_13115, AU731_17745, AU805_14740, AU830_17945, AU839_16960, AU951_10785, AU965_14440, AVA38_10850, AVB77_17860, AVB94_12475, AVC05_13710, AVC09_15555, AVD08_14940, AVD75_10490, AVD94_16345, AVG17_17440, AVL02_06935, AVL16_12105, AVM19_11045, AWT30_16365, AXM10_15020, AXM23_15980, AXR84_09155, AXU58_12665, AXX99_08590, B1265_14695, B1398_15040, B1642_12470, B1B86_13860, B1B89_12995, B1I91_14010, B1P38_06210, B1Q82_08785, B2E31_12855, B4V59_14365, B4W90_11945, B5A40_18175, B6362_19530, B6G98_09840, B6M25_12470, B6M43_11445, B7071_09685, B7890_16815, B7J30_08950, B7Q27_13330, B8Y16_13920, B8Y36_10435, B8Z46_12215, B9653_08735, B9C61_09460, B9C71_10305, B9C90_09140, B9C91_11100, B9C96_06975, B9M14_15255, B9O84_06255, B9U29_20160, BBQ66_07980, BEL47_15520, BFE55_17500, BFE61_13600, BGP52_15605, BIC00_11775, BIC01_03425, BIC03_12465, BIC13_09510, BJP89_14935, BK110_11970, BKM50_13625, BLB03_12065, BMG85_01485, BMS46_14205, BMU56_10065, BSC80_16315, BSD55_15985, BZ203_13370, BZ210_08250, BZG47_14895, BZN20_13125, BZZ88_21635, C4E88_11520, C5U54_24325, C5W43_17645, CA117_14980, CB102_02675, CB119_10390, CB161_08930, CB198_19420, CB380_13295, CB383_12585, CB416_11695, CB530_12435, CB535_09465, CB570_05200, CB646_09025, CB657_11330, CBH20_11220, CBM40_08545, CBM67_14430, CBM76_12750, CBN77_20665, CBO42_14460, CBR08_08850, CBU15_19945, CBU32_00760, CBZ90_12320, CC339_03310, CC403_05060, CC453_12125, CC594_20855, CC652_11600, CC725_10110, CC886_11620, CC918_07450, CC944_09505, CC971_10010, CCF93_15515, CCP17_10715, CCW27_14410, CD48_15270, CD977_10835, CDJ75_08265, CDQ60_11320, CDT37_13185, CDZ72_16490, CE355_08040, CE615_16735, CE70_14835, CE806_10370, CE87_12900, CE896_01015, CEC46_09750, CEC56_04870, CED07_06500, CEL48_20705, CEL55_09205, CEQ70_15765, CER78_12570, CET98_13495, CEY64_16305, CFB16_15760, CFB28_17680, CFE76_19020, CFE79_15610, CFF58_13355, CFF59_13510, CFJ48_12690, CGG73_15810, CHN22_08020, CI444_12440, CIX60_15545, CJC42_16545, CPR79_14100, CPS79_08255, CPX68_07570, CQE35_07160, CQG18_09040, CQO33_12635, CR370_10310, CRB02_10290, CSG22_12970, CVR97_09845, D3147_17580, D3174_01810, D3F31_11215, D3T68_22780, D3Y48_14800, D4361_11425, D4369_10470, D4380_14255, D4387_10710, D4422_10715, D4E62_15595, D4E68_12645, D4E74_04805, D4X64_11635, D4X79_12705, D4Y62_12305, D5823_23275, D5949_13360, D5B48_08355, D5C67_13450, D5C71_13810, D5N86_08445, D5N95_12575, D5O82_10940, D5P17_11555, D5X47_11830, D5X51_21070, D5Y28_05580, D6360_11195, D6367_13185, D6371_12525, D6373_13850, D6395_09765, D6421_13000, D6422_12760, D6J79_14230, D6K10_23715, D6P67_11555, D6Q64_13765, D6S43_13075, D6T00_11290, D6T40_07430, D7F20_11320, D7H43_01075, D7N92_12075, D7O44_13065, D8Q90_09500, D8S24_13515, D9O84_14155, DD95_02420, DJ388_15095, DJ702_13640, DK061_07980, DK631_02345, DK641_19375, DK642_13375, DK689_12355, DK696_07780, DK698_07265, DKJ10_12345, DKR95_07440, DKS55_11340, DKU45_11320, DKU57_10630, DKU80_05405, DLB14_07805, DLB57_08870, DLB93_12855, DLR28_13470, DM322_20130, DM733_21940, DMI89_06860, DMO92_13710, DMV40_11670, DMZ93_22620, DN165_13395, DN204_13780, DN359_20245, DNB97_22830, DNL62_12910, DNM27_08910, DNM63_11945, DNU59_10640, DNV08_13515, DNV12_21330, DNV30_09985, DNY92_08010, DNZ37_12590, DO350_10650, DO533_09745, DO585_12725, DO640_13295, DO698_21090, DO766_09590, DO828_16445, DO960_04625, DOC60_14865, DOH72_12230, DOI32_09640, DOI53_11380, DOI92_10015, DOJ39_13330, DOJ91_15905, DOQ54_10850, DOQ88_19075, DOR12_10695, DOV43_19010, DOW25_10390, DP680_11760, DPB42_06345, DPB45_09375, DPB48_12795, DPB57_11855, DPD91_07890, DPD95_08365, DPD99_18580, DPF41_10345, DPF68_09290, DPJ93_06885, DPK32_10835, DPK79_10855, DPL02_08725, DPP13_16840, DPP94_12530, DPP97_14020, DPS76_08870, DPT18_10485, DPU20_11590, DPY58_18740, DQ848_10815, DQ947_12275, DQ951_12780, DQC39_14690, DQC52_17465, DQD03_12025, DQD22_14205, DQE64_12330, DQE65_13455, DQK42_17635, DQQ98_14965, DQR10_20350, DQR44_12005, DQR61_11120, DQS14_10375, DQY10_09140, DQZ46_08550, DQZ56_12760, DR982_22020, DRL45_07940, DRM14_11520, DRM16_14710, DRR75_23095, DRT38_13015, DRT61_23690, DRT65_15310, DRV05_08945, DRW84_11665, DRX36_22780, DRX66_07345, DS270_18375, DS296_03655, DS451_17430, DS453_12950, DS521_10015, DS619_11600, DSF69_12145, DSF94_10460, DSG41_14570, DSM38_11155, DSN15_12590, DSR36_10905, DTE73_10415, DTF68_07740, DTG22_22525, DTG27_16445, DTW13_10745, DTW14_14950, DTW26_11965, DU071_21905, DU223_06195, DU657_07745, DU821_10140, DU879_10520, DU924_08500, DUQ28_11140, DUQ56_08490, DUQ92_13185, DUR36_14185, DUV75_15260, DUW10_15950, DUW48_09895, DVF14_11920, DVF88_08270, DVG01_14360, DVZ53_05935, DWU22_23860, DWU62_21645, DY580_21440, DYM27_06865, DYS82_09690, DZG11_20930, E0584_16370, E0595_14185, E0600_21890, E0935_14485, E0989_09310, E0M34_15895, E0S07_16310, E0U75_13640, E0V94_09045, E1336_08925, E1A11_13485, E1A20_12000, E5196_05695, E6W45_14470, EBB93_17635, EBC01_10965, EBD14_12205, EBD99_18850, EBK21_14930, EBL31_09840, EBO41_09410, EBP31_06115, EC404_15850, EC52_15480, ECA50_20460, ECC89_11785, ED424_08285, ED467_11830, EDL18_13765, EEK73_13190, EEQ30_16240, EER35_07340, EGL32_12130, EGN81_07495, EGU67_13655, EGU98_14315, EHB09_14460, EHB24_11945, EHB55_22345, EHC98_05345, EIE48_10505, EIW53_04795, EJI18_11350, EJO08_13340, EJO98_13625, EKA25_12980, EL822_07390, ELO47_09560, ELR28_08900, ELS01_12400, EM832_12680, EM840_06380, EMN66_07620, EMY79_09360, EO190_08315, EP115_18440, EP446_20135, EPB30_13505, EPH81_08120, EQG93_05510, EQG94_13030, ERM04_09810, EU306_11875, EU349_11640, EU873_21965, EUB95_05675, EUQ56_12115, EUQ65_09175, EUQ74_13570, EUS13_08790, EVT69_22445, EVY71_04215, EW905_06135, EWB18_06485, EWE52_05820, EWJ47_09340, EWZ09_13550, EXA47_07665, EXB31_05300, EXB41_09095, EYA29_15940, EYJ91_08825, F0D96_14965, F2O93_14305, F2P00_11865, F3Q46_16675, F3Q58_07850, F3Q59_15070, F3Q88_00720, F3Q97_16025, F3R12_18690, F3R61_10195, F3R63_13520, F9G02_06435, F9O44_04025, FE758_13940, FEM52_13990, FGZ46_08850, FJM64_14760, FL833_11895, FQC24_10010, FQD13_04095, FQX78_02535, GCH31_06840, GCQ81_17295, GCZ80_15980, GEZ01_10265, GW08_14750, JO10_24665, KP44_13855, LZ63_14980, NCTC13348_05301, NG02_14230, NG06_18895, NG18_08765, NU83_17610, QA89_08030, QB40_11485, QD15_11360, R035_06990, RJ78_11590, SAMEA4398682_01637, SE14_02481, Y934_23370, YG50_16765, YR17_10960, YT65_22010, Z700_22650, Z705_18140, ZB89_19920, ZC54_19680, ZT09_16805, ZT28_13365, ZT74_18075, ZT89_18160, ZU86_17815, ZU92_16805, ZV06_14780, ZV17_16185, ZV33_17250, ZV34_18355, ZV38_13400, ZV58_19590, ZV70_18315, ZV76_14470, ZV78_21800, ZV90_21250, ZW74_16110, ZX03_15750, ZY23_11835, ZY27_17660, ZY40_02770, ZY51_16230, ZZ18_15945, ZZ43_13745, ZZ77_13130, ZZ79_15595 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6zii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zii OCA], [https://pdbe.org/6zii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zii RCSB], [https://www.ebi.ac.uk/pdbsum/6zii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zii ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6zii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zii OCA], [https://pdbe.org/6zii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zii RCSB], [https://www.ebi.ac.uk/pdbsum/6zii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zii ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/C4PCU2_SALTM C4PCU2_SALTM]] Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner.[HAMAP-Rule:MF_00981]  
[https://www.uniprot.org/uniprot/RCSB_SALTY RCSB_SALTY] Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner.[HAMAP-Rule:MF_00981]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 20: Line 19:
</div>
</div>
<div class="pdbe-citations 6zii" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6zii" style="background-color:#fffaf0;"></div>
==See Also==
*[[Response regulator 3D structure|Response regulator 3D structure]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus typhimurium loeffler 1892]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Casino, P]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Huesa, J]]
[[Category: Casino P]]
[[Category: Marina, A]]
[[Category: Huesa J]]
[[Category: Dna binding protein]]
[[Category: Marina A]]
[[Category: Phosphorylation]]
[[Category: Response regulator]]
[[Category: Transcriptional factor]]
[[Category: Two-component system]]

Latest revision as of 14:52, 1 February 2024

Structure of the isolated REC domain of RcsB from Salmonella enterica serovar Typhimurium in the presence of phosphomimetic BeF3-Structure of the isolated REC domain of RcsB from Salmonella enterica serovar Typhimurium in the presence of phosphomimetic BeF3-

Structural highlights

6zii is a 2 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RCSB_SALTY Component of the Rcs signaling system, which controls transcription of numerous genes. RcsB is the response regulator that binds to regulatory DNA regions. Can function both in an RcsA-dependent or RcsA-independent manner.[HAMAP-Rule:MF_00981]

Publication Abstract from PubMed

RcsB is a transcriptional regulator that controls expression of numerous genes in enteric bacteria. RcsB accomplishes this role alone or in combination with auxiliary transcriptional factors independently or dependently of phosphorylation. To understand the mechanisms by which RcsB regulates such large number of genes, we performed structural studies as well as in vitro and in vivo functional studies with different RcsB variants. Our structural data reveal that RcsB binds promoters of target genes such as rprA and flhDC in a dimeric active conformation. In this state, the RcsB homodimer docks the DNA-binding domains into the major groove of the DNA, facilitating an initial weak read-out of the target sequence. Interestingly, comparative structural analyses also show that DNA binding may stabilize an active conformation in unphosphorylated RcsB. Furthermore, RNAseq performed in strains expressing wild-type or several RcsB variants provided new insights into the contribution of phosphorylation to gene regulation and assign a potential role of RcsB in controlling iron metabolism. Finally, we delimited the RcsB box for homodimeric active binding to DNA as the sequence TN(G/A)GAN4TC(T/C)NA. This RcsB box was found in promoter, intergenic and intragenic regions, facilitating both increased or decreased gene transcription.

Structure-based analyses of Salmonella RcsB variants unravel new features of the Rcs regulon.,Huesa J, Giner-Lamia J, Pucciarelli MG, Paredes-Martinez F, Garcia-del Portillo F, Marina A, Casino P Nucleic Acids Res. 2021 Feb 26;49(4):2357-2374. doi: 10.1093/nar/gkab060. PMID:33638994[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Huesa J, Giner-Lamia J, Pucciarelli MG, Paredes-Martinez F, Garcia-del Portillo F, Marina A, Casino P. Structure-based analyses of Salmonella RcsB variants unravel new features of the Rcs regulon. Nucleic Acids Res. 2021 Feb 26;49(4):2357-2374. doi: 10.1093/nar/gkab060. PMID:33638994 doi:http://dx.doi.org/10.1093/nar/gkab060

6zii, resolution 2.50Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA