1qpp
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(New page: 200px<br /><applet load="1qpp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qpp, resolution 2.6Å" /> '''CRYSTAL STRUCTURES OF...)
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Revision as of 22:45, 20 November 2007
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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
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