1DG4

NMR STRUCTURE OF THE SUBSTRATE BINDING DOMAIN OF DNAK IN THE APO FORM

Summary for 1DG4

• Entry DOI: 10.2210/pdb1dg4/pdb
• Related: 1DKZ 2BPR
• Descriptor: DNAK (1 entity in total)
• Functional Keywords: dnak, chaperone, substrate binding domain
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 12243.81

Authors

Pellecchia, M.,Montgomery, D.L.,Stevens, S.Y.,Van der Kooi, C.W.,Feng, H.,Gierasch, L.M.,Zuiderweg, E.R.P. (deposition date: 1999-11-23, release date: 1999-12-08, Last modification date: 2024-05-22)

Primary citation

Pellecchia, M.,Montgomery, D.L.,Stevens, S.Y.,Vander Kooi, C.W.,Feng, H.P.,Gierasch, L.M.,Zuiderweg, E.R.
Structural insights into substrate binding by the molecular chaperone DnaK.
Nat.Struct.Biol., 7:298-303, 2000

PubMed Abstract: 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.

PubMed: 10742174
DOI: 10.1038/74062

Experimental method

SOLUTION NMR