1r6c

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Revision as of 23:11, 20 November 2007

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spinqualitylabelsall models 1r6c, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

High resolution structure of ClpN

Overview

Escherichia coli ClpA, an Hsp100/Clp chaperone and an integral component, of the ATP-dependent ClpAP protease, participates in the dissolution and, degradation of regulatory proteins and protein aggregates. ClpA consists, of three functional domains: an N-terminal domain and two ATPase domains, D1 and D2. The N-domain is attached to D1 by a mobile linker and is made, up of two tightly bound, identically folded alpha-helical bundles related, by a pseudo 2-fold symmetry. Between the halves of the pseudo-dimer is a, large flexible acidic loop that becomes better ordered upon binding of the, small adaptor protein, ClpS. We have identified a number of structural, features in the N-domain, including a Zn(++) binding motif, several, interfaces for binding to ClpS, and a prominent hydrophobic surface area, that binds peptides in different configurations. These structural motifs, may contribute to binding of protein or peptide substrates with weak, affinity and broad specificity. Kinetic studies comparing wild-type ClpA, to a mutant ClpA with its N-domain deleted show that the N-domains, contribute to the binding of a non-specific protein substrate but not of a, folded substrate with the specific SsrA recognition tag. A functional, model is proposed in which the N-domains in ClpA function as tentacles to, weakly hold on to proteins thereby enhancing local substrate, concentration.

About this Structure

1R6C is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone., Xia D, Esser L, Singh SK, Guo F, Maurizi MR, J Struct Biol. 2004 Apr-May;146(1-2):166-79. PMID:15037248

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