1pdk: Difference between revisions
New page: left|200px<br /><applet load="1pdk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pdk, resolution 2.4Å" /> '''PAPD-PAPK CHAPERONE-P... |
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[[Image:1pdk.jpg|left|200px]]<br /><applet load="1pdk" size=" | [[Image:1pdk.jpg|left|200px]]<br /><applet load="1pdk" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1pdk, resolution 2.4Å" /> | caption="1pdk, resolution 2.4Å" /> | ||
'''PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS'''<br /> | '''PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS'''<br /> | ||
==Overview== | ==Overview== | ||
Many Gram-negative pathogens assemble architecturally and functionally | 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 Structure== | ==About this Structure== | ||
1PDK is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | 1PDK is a [http://en.wikipedia.org/wiki/Protein_complex 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== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Fuetterer, K.]] | [[Category: Fuetterer, K.]] | ||
[[Category: Hultgren, S | [[Category: Hultgren, S J.]] | ||
[[Category: Sauer, F | [[Category: Sauer, F G.]] | ||
[[Category: Waksman, G.]] | [[Category: Waksman, G.]] | ||
[[Category: bacterial adhesion]] | [[Category: bacterial adhesion]] | ||
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[[Category: pilus]] | [[Category: pilus]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:27:42 2008'' | ||
Revision as of 15:27, 21 February 2008
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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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