1qpp: Difference between revisions

Revision as of 06:46, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1qpp.png

Template:STRUCTURE 1qpp

CRYSTAL STRUCTURES OF SELF CAPPING PAPD CHAPERONE HOMODIMERSCRYSTAL STRUCTURES OF SELF CAPPING PAPD CHAPERONE HOMODIMERS

Template:ABSTRACT PUBMED 10393968

About this StructureAbout this Structure

1QPP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

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 Tue Jul 29 06:46:49 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1qpp.gif|left|200px]]
+{{Seed}}
+[[Image:1qpp.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1qpp|  PDB=1qpp  |  SCENE=  }}
-'''CRYSTAL STRUCTURES OF SELF CAPPING PAPD CHAPERONE HOMODIMERS'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10393968}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10393968 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10393968}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Beta barrel]]
 [[Category: Immunoglobulin fold chaperone]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:33:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:46:49 2008''