1pdk: Difference between revisions

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[[Image:1pdk.~~jpg~~|left|200px]]

[[Image:1pdk.png|left|200px]]

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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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_10446050}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10446050 is the PubMed ID number.

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==About this Structure==

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[[Category: Chaperone]]

[[Category: Pilus]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 04~~:58:00 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:15:55 2008''

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-[[Image:1pdk.jpg|left|200px]]
+{{Seed}}
+[[Image:1pdk.png|left|200px]]
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 {{STRUCTURE_1pdk|  PDB=1pdk  |  SCENE=  }}
-'''PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS'''
+===PAPD-PAPK CHAPERONE-PILUS SUBUNIT COMPLEX FROM E.COLI P PILUS===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10446050}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10446050 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10446050}}
 ==About this Structure==
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 [[Category: Chaperone]]
 [[Category: Pilus]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:58:00 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:15:55 2008''