1qpp

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|ACTIVITY=
|ACTIVITY=
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|RELATEDENTRY=[[3dpa|3dpa]], [[1qpx|1QPX]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qpp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpp OCA], [http://www.ebi.ac.uk/pdbsum/1qpp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qpp RCSB]</span>
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[[Category: immunoglobulin fold chaperone]]
[[Category: immunoglobulin fold chaperone]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:17:15 2008''

Revision as of 20:17, 30 March 2008


PDB ID 1qpp

Drag the structure with the mouse to rotate
, resolution 2.6Å
Related: 3dpa, 1QPX


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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