3ucs: Difference between revisions

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'''Unreleased structure'''
{{STRUCTURE_3ucs|  PDB=3ucs  |  SCENE=  }}
===Crystal structure of the complex between CBPA J-domain and CBPM===


The entry 3ucs is ON HOLD until Paper Publication
==Function==
[[http://www.uniprot.org/uniprot/CBPA_ECOLI CBPA_ECOLI]] DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.<ref>PMID:7601860</ref> <ref>PMID:8824642</ref>  


Authors: Shi, R., Sarraf, N.S., Cygler, M., Ekiel, I., Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI)
==About this Structure==
[[3ucs]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12] and [http://en.wikipedia.org/wiki/Klebsiella_pneumoniae_342 Klebsiella pneumoniae 342]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UCS OCA].


Description: Crystal structure of the complex between CBPA J-domain and CBPM
==Reference==
<references group="xtra"/><references/>
[[Category: Escherichia coli k-12]]
[[Category: Klebsiella pneumoniae 342]]
[[Category: BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative.]]
[[Category: Cygler, M.]]
[[Category: Ekiel, I.]]
[[Category: Sarraf, N S.]]
[[Category: Shi, R.]]
[[Category: Bsgi]]
[[Category: Chaperone]]
[[Category: Co-chaperone regulation]]
[[Category: Montreal-kingston bacterial structural genomics initiative]]
[[Category: Protein-protein complex]]
[[Category: Structural genomic]]

Revision as of 14:11, 3 July 2013

Template:STRUCTURE 3ucs

Crystal structure of the complex between CBPA J-domain and CBPM

Function

[CBPA_ECOLI] DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM.[1] [2]

About this Structure

3ucs is a 4 chain structure with sequence from Escherichia coli k-12 and Klebsiella pneumoniae 342. Full crystallographic information is available from OCA.

Reference

  1. ↑ Ueguchi C, Shiozawa T, Kakeda M, Yamada H, Mizuno T. A study of the double mutation of dnaJ and cbpA, whose gene products function as molecular chaperones in Escherichia coli. J Bacteriol. 1995 Jul;177(13):3894-6. PMID:7601860
  2. ↑ Wegrzyn A, Taylor K, Wegrzyn G. The cbpA chaperone gene function compensates for dnaJ in lambda plasmid replication during amino acid starvation of Escherichia coli. J Bacteriol. 1996 Oct;178(19):5847-9. PMID:8824642

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