1pdk: Difference between revisions
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[[Image:1pdk.jpg|left|200px]] | [[Image:1pdk.jpg|left|200px]] | ||
'''PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS''' | {{Structure | ||
|PDB= 1pdk |SIZE=350|CAPTION= <scene name='initialview01'>1pdk</scene>, resolution 2.4Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1PDK is a [ | 1PDK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PDK OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10446050 10446050] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: pilus]] | [[Category: pilus]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:23:02 2008'' |
Revision as of 14:23, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS
OverviewOverview
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.
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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