1pdk: Difference between revisions

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{{STRUCTURE_1pdk|  PDB=1pdk  |  SCENE=  }}  
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'''PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS'''
===PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS===




==Overview==
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Many Gram-negative pathogens assemble architecturally and functionally diverse adhesive pili on their surfaces by the chaperone-usher pathway. Immunoglobulin-like periplasmic chaperones escort pilus subunits to the usher, a large protein complex that facilitates the translocation and assembly of subunits across the outer membrane. The crystal structure of the PapD-PapK chaperone-subunit complex, determined at 2.4 angstrom resolution, reveals that the chaperone functions by donating its G(1) beta strand to complete the immunoglobulin-like fold of the subunit via a mechanism termed donor strand complementation. The structure of the PapD-PapK complex also suggests that during pilus biogenesis, every subunit completes the immunoglobulin-like fold of its neighboring subunit via a mechanism termed donor strand exchange.
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==About this Structure==
==About this Structure==
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[[Category: Chaperone]]
[[Category: Chaperone]]
[[Category: Pilus]]
[[Category: Pilus]]
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Revision as of 19:15, 28 July 2008

File:1pdk.png

Template:STRUCTURE 1pdk

PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUSPAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS

Template:ABSTRACT PUBMED 10446050

About this StructureAbout this Structure

1PDK is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of chaperone function and pilus biogenesis., Sauer FG, Futterer K, Pinkner JS, Dodson KW, Hultgren SJ, Waksman G, Science. 1999 Aug 13;285(5430):1058-61. PMID:10446050

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