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| - | [[Image:2os7.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2os7| PDB=2os7 | SCENE= }} | | {{STRUCTURE_2os7| PDB=2os7 | SCENE= }} |
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| - | '''Caf1M periplasmic chaperone tetramer'''
| + | ===Caf1M periplasmic chaperone tetramer=== |
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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_17376079}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17376079 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17376079}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hetero beta barrel]] | | [[Category: Hetero beta barrel]] |
| | [[Category: Immunoglobulin fold]] | | [[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 Mon Jul 28 02:27:45 2008'' |
Revision as of 23:27, 27 July 2008
Template:STRUCTURE 2os7
Caf1M periplasmic chaperone tetramer
Template:ABSTRACT PUBMED 17376079
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 Mon Jul 28 02:27:45 2008
