1m5y
From Proteopedia
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<StructureSection load='1m5y' size='340' side='right'caption='[[1m5y]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1m5y' size='340' side='right'caption='[[1m5y]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1m5y]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1m5y]] is a 4 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=1M5Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M5Y 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]] 3Å</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m5y OCA], [https://pdbe.org/1m5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m5y RCSB], [https://www.ebi.ac.uk/pdbsum/1m5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m5y 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=1m5y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m5y OCA], [https://pdbe.org/1m5y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m5y RCSB], [https://www.ebi.ac.uk/pdbsum/1m5y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m5y ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/SURA_ECOLI SURA_ECOLI] Chaperone involved in the correct folding and assembly of outer membrane proteins, such as OmpA, OmpF and LamB. Recognizes specific patterns of aromatic residues and the orientation of their side chains, which are found more frequently in integral outer membrane proteins. May act in both early periplasmic and late outer membrane-associated steps of protein maturation. Essential for the survival of E.coli in stationary phase. Required for pilus biogenesis.<ref>PMID:2165476</ref> <ref>PMID:8985185</ref> <ref>PMID:11226178</ref> <ref>PMID:16267292</ref> | |
== 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=1m5y 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=1m5y ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The SurA protein facilitates correct folding of outer membrane proteins in gram-negative bacteria. The sequence of Escherichia coli SurA presents four segments, two of which are peptidyl-prolyl isomerases (PPIases); the crystal structure reveals an asymmetric dumbbell, in which the amino-terminal, carboxy-terminal, and first PPIase segments of the sequence form a core structural module, and the second PPIase segment is a satellite domain tethered approximately 30 A from this module. The core module, which is implicated in membrane protein folding, has a novel fold that includes an extended crevice. Crystal contacts show that peptides bind within the crevice, suggesting a model for chaperone activity whereby segments of polypeptide may be repetitively sequestered and released during the membrane protein-folding process. | ||
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| - | Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins.,Bitto E, McKay DB Structure. 2002 Nov;10(11):1489-98. PMID:12429090<ref>PMID:12429090</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1m5y" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | + | [[Category: Bitto E]] | |
| - | [[Category: Bitto | + | [[Category: McKay DB]] |
| - | [[Category: McKay | + | |
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Current revision
Crystallographic Structure of SurA, a Molecular Chaperone that Facilitates Outer Membrane Porin Folding
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