2os7
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2os7.gif|left|200px]] | [[Image:2os7.gif|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2os7", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2os7| PDB=2os7 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''Caf1M periplasmic chaperone tetramer''' | '''Caf1M periplasmic chaperone tetramer''' | ||
| Line 27: | Line 24: | ||
[[Category: Knight, S D.]] | [[Category: Knight, S D.]] | ||
[[Category: Zavialov, A Z.]] | [[Category: Zavialov, A Z.]] | ||
| - | [[Category: | + | [[Category: Hetero beta barrel]] |
| - | [[Category: | + | [[Category: Immunoglobulin fold]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:33:23 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:33, 4 May 2008
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 Page seeded by OCA on Sun May 4 11:33:23 2008
