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PDBsum entry 3dpb
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Chaperone/structural protein
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PDB id
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3dpb
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Contents |
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196 a.a.
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149 a.a.
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128 a.a.
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* Residue conservation analysis
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PDB id:
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| Name: |
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Chaperone/structural protein
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Title:
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Crystal structure of the complex of the caf1m chaperone with the mini- fiber of two caf1 subunits (caf1:caf1), carrying the ala9val, ala11val, and leu13val mutations in the gd donor strand
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Structure:
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Chaperone protein caf1m. Chain: a. Fragment: unp residues 24 to 258. Synonym: capsule protein fraction 1 machinery. Engineered: yes. F1 capsule antigen. Chain: b, c. Fragment: unp residues22 to 170. Engineered: yes.
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Source:
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Yersinia pestis. Organism_taxid: 632. Gene: caf1m, ypmt1.82, y5194, y1098, yp_pmt084. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: caf1, ypmt1.84, y5196, y1100, yp_pmt082. Expression_system_taxid: 562
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Resolution:
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2.20Å
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R-factor:
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0.201
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R-free:
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0.244
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Authors:
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L.J.Fooks,X.Yu,E.Moslehi-Mohebi,V.Tischenko,S.D.Knight,S.Macintyre, A.V.Zavialov
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Key ref:
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L.J.Fooks
et al.
Hydrophobicity and rigidity of binding segments enable caf1m chaperone to act as assembly catalyst.
To be published,
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Date:
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07-Jul-08
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Release date:
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14-Jul-09
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PROCHECK
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Headers
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References
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P26926
(CAF1M_YERPE) -
Chaperone protein caf1M from Yersinia pestis
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Seq:
Struc:
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258 a.a.
196 a.a.
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Links
