1qpp: Difference between revisions

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[[Image:1qpp.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_1qpp|  PDB=1qpp  |  SCENE=  }}  
{{STRUCTURE_1qpp|  PDB=1qpp  |  SCENE=  }}  


'''CRYSTAL STRUCTURES OF SELF CAPPING PAPD CHAPERONE HOMODIMERS'''
===CRYSTAL STRUCTURES OF SELF CAPPING PAPD CHAPERONE HOMODIMERS===




==Overview==
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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.
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{{ABSTRACT_PUBMED_10393968}}


==About this Structure==
==About this Structure==
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[[Category: Beta barrel]]
[[Category: Beta barrel]]
[[Category: Immunoglobulin fold chaperone]]
[[Category: Immunoglobulin fold chaperone]]
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