2os7
From Proteopedia
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| - | [[Image:2os7.gif|left|200px]] | + | [[Image:2os7.gif|left|200px]] |
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| - | '''Caf1M periplasmic chaperone tetramer''' | + | {{Structure |
| + | |PDB= 2os7 |SIZE=350|CAPTION= <scene name='initialview01'>2os7</scene>, resolution 2.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= caf1M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 Yersinia pestis]) | ||
| + | }} | ||
| + | |||
| + | '''Caf1M periplasmic chaperone tetramer''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2OS7 is a [ | + | 2OS7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OS7 OCA]. |
==Reference== | ==Reference== | ||
| - | A novel self-capping mechanism controls aggregation of periplasmic chaperone Caf1M., Zavialov AV, Knight SD, Mol Microbiol. 2007 Apr;64(1):153-64. PMID:[http:// | + | A novel self-capping mechanism controls aggregation of periplasmic chaperone Caf1M., Zavialov AV, Knight SD, Mol Microbiol. 2007 Apr;64(1):153-64. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17376079 17376079] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Yersinia pestis]] | [[Category: Yersinia pestis]] | ||
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[[Category: immunoglobulin fold]] | [[Category: immunoglobulin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:03:47 2008'' |
Revision as of 16:03, 20 March 2008
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| , resolution 2.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | caf1M (Yersinia pestis) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Caf1M periplasmic chaperone tetramer
Overview
The chaperone Caf1M belongs to a family of ATP-independent periplasmic chaperones that together with outer membrane ushers assemble and secrete filamentous adhesion organelles in Gram-negative pathogens. It assists in folding and transport of Caf1 subunits of the F1 capsular antigen of Yersinia pestis, the microbe causing bubonic plague. In the periplasm, Caf1M prevents subunit aggregation by capping the extensive hydrophobic surface of activated Caf1. We found that subunit-free Caf1M exists predominantly as a tetramer [K(d) = (2-30) x 10(-14) M(3) in the 12-37 degrees C interval]. A 2.9 A resolution crystal structure of the Caf1M tetramer reveals that each of the four molecules contribute its subunit binding sequences (the A(1) and G(1) strands) to form an eight-stranded hetero-sandwich with a well-packed phenylalanine-rich hydrophobic core. Tetramerization protects chaperone molecules against enzymatic proteolysis. Deletions in the subunit binding motifs completely abolish tetramer assembly, suggesting that the hetero-sandwich is the main structural feature holding the tetramer together. Arresting tetramer assembly by a deletion of the N-terminal binding motif, while leaving the major subunit binding motif VGVFVQFAI (G(1) strand) intact, results in accumulation of unspecific aggregates. Deletions in the VGVFVQFAI motif abolish both tetramer assembly and aggregation, consistent with the predicted high beta-aggregation propensity for this motif. These results suggest that the packing of the aggregation-prone subunit binding sequences into the hetero-domain is a novel molecular mechanism preventing unspecific aggregation of the free chaperone.
About this Structure
2OS7 is a Single protein structure of sequence from Yersinia pestis. Full crystallographic information is available from OCA.
Reference
A novel self-capping mechanism controls aggregation of periplasmic chaperone Caf1M., Zavialov AV, Knight SD, Mol Microbiol. 2007 Apr;64(1):153-64. PMID:17376079
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