1dg4
From Proteopedia
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NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK IN THE APO FORM
Overview
How substrate affinity is modulated by nucleotide binding remains a, fundamental, unanswered question in the study of 70 kDa heat shock protein, (Hsp70) molecular chaperones. We find here that the Escherichia coli, Hsp70, DnaK, lacking the entire alpha-helical domain, DnaK(1-507), retains, the ability to support lambda phage replication in vivo and to pass, information from the nucleotide binding domain to the substrate binding, domain, and vice versa, in vitro. We determined the NMR solution structure, of the corresponding substrate binding domain, DnaK(393-507), without, substrate, and assessed the impact of substrate binding. Without bound, substrate, loop L3,4 and strand beta3 are in significantly different, conformations than observed in previous structures of the bound DnaK, substrate binding domain, leading to occlusion of the substrate binding, site. Upon substrate binding, the beta-domain shifts towards the structure, seen in earlier X-ray and NMR structures. Taken together, our results, suggest that conformational changes in the beta-domain itself contribute, to the mechanism by which nucleotide binding modulates substrate binding, affinity.
About this Structure
1DG4 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural insights into substrate binding by the molecular chaperone DnaK., Pellecchia M, Montgomery DL, Stevens SY, Vander Kooi CW, Feng HP, Gierasch LM, Zuiderweg ER, Nat Struct Biol. 2000 Apr;7(4):298-303. PMID:10742174
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