3ny7: Difference between revisions

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 <StructureSection load='3ny7' size='340' side='right'caption='[[3ny7]], [[Resolution|resolution]] 1.92&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ny7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895] and [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NY7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ny7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NY7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NY7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SXM:3-{[2-({N-[(2S)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)BUTANOYL]-BETA-ALANYL}AMINO)ETHYL]SULFANYL}-3-OXOPROPANOIC+ACID'>SXM</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]] 1.922&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ychM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SXM:3-{[2-({N-[(2S)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)BUTANOYL]-BETA-ALANYL}AMINO)ETHYL]SULFANYL}-3-OXOPROPANOIC+ACID'>SXM</scene></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=3ny7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ny7 OCA], [https://pdbe.org/3ny7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ny7 RCSB], [https://www.ebi.ac.uk/pdbsum/3ny7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ny7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/C6EHC0_ECOBD C6EHC0_ECOBD]] Carrier of the growing fatty acid chain in fatty acid biosynthesis.[RuleBase:RU003545]
+[https://www.uniprot.org/uniprot/DAUA_ECOLI DAUA_ECOLI] Responsible for the aerobic transport of succinate from the periplasm to the cytoplasm at acidic pH (PubMed:23278959). Can transport other C4-dicarboxylic acids such as aspartate and fumarate (PubMed:23278959). May also play a role in the regulation of C4-dicarboxylic acid metabolism at pH 7, via regulation of expression and/or activity of DctA. May act as a co-sensor of DcuS (PubMed:23278959).<ref>PMID:23278959</ref>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Escherichia coli YchM is a member of the SLC26 (SulP) family of anion transporters with an N-terminal membrane domain and a C-terminal cytoplasmic STAS domain. Mutations in human members of the SLC26 family, including their STAS domain, are linked to a number of inherited diseases. Herein, we describe the high-resolution crystal structure of the STAS domain from E. coli YchM isolated in complex with acyl-carrier protein (ACP), an essential component of the fatty acid biosynthesis (FAB) pathway. A genome-wide genetic interaction screen showed that a ychM null mutation is synthetically lethal with mutant alleles of genes (fabBDHGAI) involved in FAB. Endogenous YchM also copurified with proteins involved in fatty acid metabolism. Furthermore, a deletion strain lacking ychM showed altered cellular bicarbonate incorporation in the presence of NaCl and impaired growth at alkaline pH. Thus, identification of the STAS-ACP complex suggests that YchM sequesters ACP to the bacterial membrane linking bicarbonate transport with fatty acid metabolism.
-Structure of a SLC26 anion transporter STAS domain in complex with acyl carrier protein: implications for E. coli YchM in fatty acid metabolism.,Babu M, Greenblatt JF, Emili A, Strynadka NC, Reithmeier RA, Moraes TF Structure. 2010 Nov 10;18(11):1450-62. PMID:21070944<ref>PMID:21070944</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3ny7" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 26: / Line 17: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
 [[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Moraes, T F]]
+[[Category: Moraes TF]]
-[[Category: Reithmeier, R]]
+[[Category: Reithmeier R]]
-[[Category: Strynadka, N C.S]]
+[[Category: Strynadka NCS]]
-[[Category: 4'-phosphopantetheine]]
-[[Category: Acyl carrier protein]]
-[[Category: Anion transport]]
-[[Category: Bicarbonate transport]]
-[[Category: Membrane protein]]
-[[Category: Ser 36 of acp]]
-[[Category: Slc26]]
-[[Category: Stas domain]]
-[[Category: Ychm]]