1qpp
From Proteopedia
(New page: 200px<br /><applet load="1qpp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qpp, resolution 2.6Å" /> '''CRYSTAL STRUCTURES OF...) |
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| - | [[Image:1qpp.gif|left|200px]]<br /><applet load="1qpp" size=" | + | [[Image:1qpp.gif|left|200px]]<br /><applet load="1qpp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qpp, resolution 2.6Å" /> | caption="1qpp, resolution 2.6Å" /> | ||
'''CRYSTAL STRUCTURES OF SELF CAPPING PAPD CHAPERONE HOMODIMERS'''<br /> | '''CRYSTAL STRUCTURES OF SELF CAPPING PAPD CHAPERONE HOMODIMERS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | PapD is an immunoglobulin-like chaperone that mediates the assembly of P | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1QPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http:// | + | 1QPP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=1QPP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hultgren, S | + | [[Category: Hultgren, S J.]] |
| - | [[Category: Hung, D | + | [[Category: Hung, D L.]] |
| - | [[Category: Knight, S | + | [[Category: Knight, S D.]] |
| - | [[Category: Pinkner, J | + | [[Category: Pinkner, J S.]] |
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: immunoglobulin fold chaperone]] | [[Category: immunoglobulin fold chaperone]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:21 2008'' |
Revision as of 12:42, 21 February 2008
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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.
About this Structure
1QPP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural basis of chaperone self-capping in P pilus biogenesis., Hung DL, Pinkner JS, Knight SD, Hultgren SJ, Proc Natl Acad Sci U S A. 1999 Jul 6;96(14):8178-83. PMID:10393968
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