1qpx
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[3dpa|3dpa]], [[1qpp|1QPP]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpx OCA], [http://www.ebi.ac.uk/pdbsum/1qpx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qpx RCSB]</span> | ||
}} | }} | ||
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[[Category: immunoglobulin fold]] | [[Category: immunoglobulin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:17:20 2008'' |
Revision as of 20:17, 30 March 2008
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| , resolution 2.4Å | |||||||
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| Related: | 3dpa, 1QPP
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| 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
1QPX 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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