1z9s

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[[Image:1z9s.gif|left|200px]]<br /><applet load="1z9s" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1z9s.gif|left|200px]]
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caption="1z9s, resolution 2.2&Aring;" />
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'''Crystal Structure of the native chaperone:subunit:subunit Caf1M:Caf1:Caf1 complex'''<br />
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{{Structure
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|PDB= 1z9s |SIZE=350|CAPTION= <scene name='initialview01'>1z9s</scene>, resolution 2.2&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE= caf1M ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 Yersinia pestis]), caf1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 Yersinia pestis])
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}}
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'''Crystal Structure of the native chaperone:subunit:subunit Caf1M:Caf1:Caf1 complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1Z9S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z9S OCA].
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1Z9S is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z9S OCA].
==Reference==
==Reference==
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Resolving the energy paradox of chaperone/usher-mediated fibre assembly., Zavialov AV, Tischenko VM, Fooks LJ, Brandsdal BO, Aqvist J, Zav'yalov VP, Macintyre S, Knight SD, Biochem J. 2005 Aug 1;389(Pt 3):685-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15799718 15799718]
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Resolving the energy paradox of chaperone/usher-mediated fibre assembly., Zavialov AV, Tischenko VM, Fooks LJ, Brandsdal BO, Aqvist J, Zav'yalov VP, Macintyre S, Knight SD, Biochem J. 2005 Aug 1;389(Pt 3):685-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15799718 15799718]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Yersinia pestis]]
[[Category: Yersinia pestis]]
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[[Category: native minimal fiber]]
[[Category: native minimal fiber]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:30 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:32:55 2008''

Revision as of 13:32, 20 March 2008


PDB ID 1z9s

Drag the structure with the mouse to rotate
, resolution 2.2Å
Gene: caf1M (Yersinia pestis), caf1 (Yersinia pestis)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the native chaperone:subunit:subunit Caf1M:Caf1:Caf1 complex


Overview

Periplasmic chaperone/usher machineries are used for assembly of filamentous adhesion organelles of Gram-negative pathogens in a process that has been suggested to be driven by folding energy. Structures of mutant chaperone-subunit complexes revealed a final folding transition (condensation of the subunit hydrophobic core) on the release of organelle subunit from the chaperone-subunit pre-assembly complex and incorporation into the final fibre structure. However, in view of the large interface between chaperone and subunit in the pre-assembly complex and the reported stability of this complex, it is difficult to understand how final folding could release sufficient energy to drive assembly. In the present paper, we show the X-ray structure for a native chaperone-fibre complex that, together with thermodynamic data, shows that the final folding step is indeed an essential component of the assembly process. We show that completion of the hydrophobic core and incorporation into the fibre results in an exceptionally stable module, whereas the chaperone-subunit pre-assembly complex is greatly destabilized by the high-energy conformation of the bound subunit. This difference in stabilities creates a free energy potential that drives fibre formation.

About this Structure

1Z9S is a Protein complex structure of sequences from Yersinia pestis. Full crystallographic information is available from OCA.

Reference

Resolving the energy paradox of chaperone/usher-mediated fibre assembly., Zavialov AV, Tischenko VM, Fooks LJ, Brandsdal BO, Aqvist J, Zav'yalov VP, Macintyre S, Knight SD, Biochem J. 2005 Aug 1;389(Pt 3):685-94. PMID:15799718

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