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'''CRYSTAL STRUCTURES OF SELF CAPPING PAPD CHAPERONE HOMODIMERS''' | '''CRYSTAL STRUCTURES OF SELF CAPPING PAPD CHAPERONE HOMODIMERS''' | ||
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[[Category: Knight, S D.]] | [[Category: Knight, S D.]] | ||
[[Category: Pinkner, J S.]] | [[Category: Pinkner, J S.]] | ||
[[Category: | [[Category: Beta barrel]] | ||
[[Category: | [[Category: Immunoglobulin fold chaperone]] | ||
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Revision as of 03:33, 3 May 2008
CRYSTAL STRUCTURES OF SELF CAPPING PAPD CHAPERONE HOMODIMERS
Overview
PapD is an immunoglobulin-like chaperone that mediates the assembly of P pili in uropathogenic strains of Escherichia coli. It binds and caps interactive surfaces on pilus subunits to prevent their premature associations in the periplasm. We elucidated the structural basis of a mechanism whereby PapD also interacts with itself, capping its own subunit binding surface. Crystal structures of dimeric forms of PapD revealed that this self-capping mechanism involves a rearrangement and ordering of the C2-D2 and F1-G1 loops upon dimerization which might ensure that a stable dimer is not formed in solution in spite of a relatively large dimer interface. An analysis of site directed mutations revealed that chaperone dimerization requires the same surface that is otherwise used to bind subunits.
About this Structure
1QPP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural basis of chaperone self-capping in P pilus biogenesis., Hung DL, Pinkner JS, Knight SD, Hultgren SJ, Proc Natl Acad Sci U S A. 1999 Jul 6;96(14):8178-83. PMID:10393968 Page seeded by OCA on Sat May 3 06:33:37 2008
