1gzf

From Proteopedia

Revision as of 08:50, 30 October 2007

STRUCTURE OF THE CLOSTRIDIUM BOTULINUM C3 EXOENZYME (WILD-TYPE) IN COMPLEX WITH NAD

Overview

We have solved the crystal structures of Clostridium botulinum C3, exoenzyme free and complexed to NAD in the same crystal form, at 2.7 and, 1.95 A, respectively. The asymmetric unit contains four molecules, which, in the free form, share the same conformation. Upon NAD binding, C3, underwent various conformational changes, whose amplitudes were, differentially limited in the four molecules of the crystal unit. A major, rearrangement concerns the loop that contains the functionally important, ARTT motif (ADP-ribosyltransferase toxin turn-turn). The ARTT loop, undergoes an ample swinging motion to adopt a conformation that covers the, nicotinamide moiety of NAD. In particular, Gln-212, which belongs to the, ARTT motif, flips over from a solvent-exposed environment to a buried, conformation ... [(full description)]

About this Structure

1GZF is a [Single protein] structure of sequence from [Clostridium botulinum] with SO4, NAD, NIR and ADP as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

NAD binding induces conformational changes in Rho ADP-ribosylating clostridium botulinum C3 exoenzyme., Menetrey J, Flatau G, Stura EA, Charbonnier JB, Gas F, Teulon JM, Le Du MH, Boquet P, Menez A, J Biol Chem. 2002 Aug 23;277(34):30950-7. Epub 2002 May 23. PMID:12029083

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