3gz1
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Crystal structure of IpgC in complex with the chaperone binding region of IpaB== |
| - | <StructureSection load='3gz1' size='340' side='right'caption='[[3gz1]]' scene=''> | + | <StructureSection load='3gz1' size='340' side='right'caption='[[3gz1]], [[Resolution|resolution]] 2.15Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3gz1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GZ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GZ1 FirstGlance]. <br> |
| - | </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=3gz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gz1 OCA], [https://pdbe.org/3gz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gz1 RCSB], [https://www.ebi.ac.uk/pdbsum/3gz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gz1 ProSAT]</span></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]] 2.15Å</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></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=3gz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gz1 OCA], [https://pdbe.org/3gz1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gz1 RCSB], [https://www.ebi.ac.uk/pdbsum/3gz1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gz1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/IPGC_SHIFL IPGC_SHIFL] Assists the correct folding of nascent IpaB. Once it is bound to IpaB, it binds to IpaC and impedes their premature association that would lead to their degradation in the absence of IpcG. | ||
== 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=3gz1 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=3gz1 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The delivery of virulence factors into host cells through type III secretion systems is essential for enterobacterial pathogenesis. Molecular chaperones bind specifically to virulence factors in the bacterial cytosol before secretion. Invasion plasmid gene C (IpgC) is a chaperone that binds 2 essential virulence factors of Shigella: invasion plasmid antigens (Ipa) B and C. Here, we report the crystal structure of IpgC alone and in complex with the chaperone binding domain (CBD) of IpaB. The chaperone captures the CBD in an extended conformation that is stabilized by conserved residues lining the cleft. Analysis of the cocrystal structure reveals a sequence motif that is functional in the IpaB translocator class from different bacteria as determined by isothermal titration calorimetry. Our results show how translocators are chaperoned and may allow the design of inhibitors of enterobacterial diseases. | ||
| + | |||
| + | IpaB-IpgC interaction defines binding motif for type III secretion translocator.,Lunelli M, Lokareddy RK, Zychlinsky A, Kolbe M Proc Natl Acad Sci U S A. 2009 May 28. PMID:19478065<ref>PMID:19478065</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3gz1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Shigella flexneri]] |
| + | [[Category: Kolbe M]] | ||
| + | [[Category: Lokareddy RK]] | ||
| + | [[Category: Lunelli M]] | ||
| + | [[Category: Zychlinsky A]] | ||
Revision as of 15:46, 1 November 2023
Crystal structure of IpgC in complex with the chaperone binding region of IpaB
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