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==Crystal Structure of YsxC complexed with GMPPNP==
==Crystal Structure of YsxC complexed with GMPPNP==
<StructureSection load='1svw' size='340' side='right' caption='[[1svw]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='1svw' size='340' side='right'caption='[[1svw]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1svw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SVW FirstGlance]. <br>
<table><tr><td colspan='2'>[[1svw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SVW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <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]] 2.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1svl|1svl]], [[1sui|1sui]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</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">YsxC, ENGB, BSU28190 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</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=1svw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svw OCA], [https://pdbe.org/1svw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1svw RCSB], [https://www.ebi.ac.uk/pdbsum/1svw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1svw ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1svw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1svw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1svw RCSB], [http://www.ebi.ac.uk/pdbsum/1svw PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ENGB_BACSU ENGB_BACSU]] Necessary for normal cell division and for the maintenance of normal septation (By similarity).[HAMAP-Rule:MF_00321]  Binds GTP and GDP.[HAMAP-Rule:MF_00321]  
[https://www.uniprot.org/uniprot/ENGB_BACSU ENGB_BACSU] Necessary for normal cell division and for the maintenance of normal septation (By similarity).[HAMAP-Rule:MF_00321]  Binds GTP and GDP.[HAMAP-Rule:MF_00321]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sv/1svw_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sv/1svw_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1svw ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Genetic analysis has suggested that the product of the Bacillus subtilis ysxC gene is essential for survival of the microorganism and hence may represent a target for the development of a novel anti-infective agent. B.subtilis YsxC is a member of the translation factor related class of GTPases and its crystal structure has been determined in an apo form and in complex with GDP and GMPPNP/Mg2+. Analysis of these structures has allowed us to examine the conformational changes that occur during the process of nucleotide binding and GTP hydrolysis. These structural changes particularly affect parts of the switch I and switch II region of YsxC, which become ordered and disordered, respectively in the "closed" or "on" GTP-bound state and disordered and ordered, respectively, in the "open" or "off" GDP-bound conformation. Finally, the binding of the magnesium cation results in subtle shifts of residues in the G3 region, at the start of switch II, which serve to optimize the interaction with a key aspartic acid residue. The structural flexibility observed in YsxC is likely to contribute to the role of the protein, possibly allowing transduction of an essential intracellular signal, which may be mediated via interactions with a conserved patch of surface-exposed, basic residues that lies adjacent to the GTP-binding site.
Analysis of the open and closed conformations of the GTP-binding protein YsxC from Bacillus subtilis.,Ruzheinikov SN, Das SK, Sedelnikova SE, Baker PJ, Artymiuk PJ, Garcia-Lara J, Foster SJ, Rice DW J Mol Biol. 2004 May 28;339(2):265-78. PMID:15136032<ref>PMID:15136032</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[GTP-binding protein|GTP-binding protein]]
*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Artymiuk, P J]]
[[Category: Large Structures]]
[[Category: Baker, P J]]
[[Category: Artymiuk PJ]]
[[Category: Das, S K]]
[[Category: Baker PJ]]
[[Category: Foster, S J]]
[[Category: Das SK]]
[[Category: Garcia-Lara, J]]
[[Category: Foster SJ]]
[[Category: Rice, D W]]
[[Category: Garcia-Lara J]]
[[Category: Ruzheinikov, S N]]
[[Category: Rice DW]]
[[Category: Sedelnikova, S E]]
[[Category: Ruzheinikov SN]]
[[Category: Gmppnp]]
[[Category: Sedelnikova SE]]
[[Category: Gtp]]
[[Category: Gtp-binding protein]]
[[Category: Gtpase]]
[[Category: Hydrolase]]
[[Category: Ysxc]]

Latest revision as of 11:34, 14 February 2024

Crystal Structure of YsxC complexed with GMPPNPCrystal Structure of YsxC complexed with GMPPNP

Structural highlights

1svw is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.8Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ENGB_BACSU Necessary for normal cell division and for the maintenance of normal septation (By similarity).[HAMAP-Rule:MF_00321] Binds GTP and GDP.[HAMAP-Rule:MF_00321]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1svw, resolution 2.80Å

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