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3ucs
From Proteopedia
Contents |
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
- ↑ 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
- ↑ 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
Categories: Escherichia coli k-12 | Klebsiella pneumoniae 342 | BSGI, Montreal-Kingston Bacterial Structural Genomics Initiative. | Cygler, M. | Ekiel, I. | Sarraf, N S. | Shi, R. | Bsgi | Chaperone | Co-chaperone regulation | Montreal-kingston bacterial structural genomics initiative | Protein-protein complex | Structural genomic
