1qpx: Difference between revisions

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~~'''~~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.

The line below this paragraph, {{ABSTRACT_PUBMED_10393968}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10393968 is the PubMed ID number.

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==About this Structure==

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[[Category: Chaperone]]

[[Category: Immunoglobulin fold]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 06~~:34:04 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:07:20 2008''

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-[[Image:1qpx.jpg|left|200px]]
+{{Seed}}
+[[Image:1qpx.png|left|200px]]
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 {{STRUCTURE_1qpx|  PDB=1qpx  |  SCENE=  }}
-'''CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS'''
+===CRYSTAL STRUCTURES OF SELF-CAPPING PAPD CHAPERONE HOMODIMERS===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10393968}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10393968 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10393968}}
 ==About this Structure==
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 [[Category: Chaperone]]
 [[Category: Immunoglobulin fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:34:04 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:07:20 2008''