3n54
From Proteopedia
(Difference between revisions)
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==Crystal Structure of the GerBC protein== | ==Crystal Structure of the GerBC protein== | ||
- | <StructureSection load='3n54' size='340' side='right' caption='[[3n54]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='3n54' size='340' side='right'caption='[[3n54]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3n54]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3n54]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N54 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N54 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
- | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3n54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n54 OCA], [https://pdbe.org/3n54 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n54 RCSB], [https://www.ebi.ac.uk/pdbsum/3n54 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n54 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/GERBC_BACSU GERBC_BACSU] Involved in the response to the germinative mixture of L-asparagine, glucose, fructose and potassium ions (AGFK). Cannot stimulate germination in the absence of gerD and gerK gene products (fructose and glucose receptors respectively). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=3n54 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=3n54 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The nutrient germinant receptors (nGRs) of spores of Bacillus species are clusters of three proteins that play a critical role in triggering the germination of dormant spores in response to specific nutrient molecules. Here, we report the crystal structure of the C protein of the GerB germinant receptor, so-called GerBC, of Bacillus subtilis spores at 2.3 A resolution. The GerBC protein adopts a previously uncharacterized type of protein fold consisting of three distinct domains, each of which is centered by a beta sheet surrounded by multiple alpha helices. Secondary-structure prediction and structure-based sequence alignment suggest that the GerBC structure represents the prototype for C subunits of nGRs from spores of all Bacillales and Clostridiales species and defines two highly conserved structural regions in this family of proteins. GerBC forms an interlocked dimer in the crystalline state but is predominantly monomeric in solution, pointing to the possibility that GerBC oligomerizes as a result of either high local protein concentrations or interaction with other nGR proteins in spores. Our findings provide the first structural view of the nGR subunits and a molecular framework for understanding the architecture, conservation, and function of nGRs. | ||
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- | Crystal Structure of the GerBC Component of a Bacillus subtilis Spore Germinant Receptor.,Li Y, Setlow B, Setlow P, Hao B J Mol Biol. 2010 Sep 10;402(1):8-16. Epub 2010 Jul 21. PMID:20654628<ref>PMID:20654628</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 3n54" style="background-color:#fffaf0;"></div> | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] |
- | [[Category: Hao | + | [[Category: Large Structures]] |
- | [[Category: Li | + | [[Category: Hao B]] |
- | [[Category: Setlow | + | [[Category: Li Y]] |
- | [[Category: Setlow | + | [[Category: Setlow B]] |
- | + | [[Category: Setlow P]] | |
- | + |
Current revision
Crystal Structure of the GerBC protein
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