1sgk

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[[Category: transferase]]
[[Category: transferase]]
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Revision as of 13:59, 30 October 2007


1sgk, resolution 2.3Å

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NUCLEOTIDE-FREE DIPHTHERIA TOXIN

Overview

The crystal structure of diphtheria toxin (DT) in the absence of, nucleotide (nucleotide-free DT) has been determined at 2.3 A resolution to, a crystallographic R factor and free R factor of 18.2 and 28.2%, respectively. A comparison of this structure to the previously determined, structures of DT in complex with adenyly(3'-5')uridine monophosphate, (ApUp) and DT in complex with nicotinamide adenine dinucleotide (NAD), reveals that there are no significant movements of the two subdomains of, the catalytic (C) domain associated with dinucleotide binding. The side, chains of six residues within the active-site cleft, including Tyr65, Pro38, Tyr27, Thr23, Glu148, and Tyr54, show movements of up to 3 A upon, dinucleotide binding. In the structure of nucleotide-free DT, the, active-site loop ... [(full description)]

About this Structure

1SGK is a [Single protein] structure of sequence from [Corynephage beta]. Active as [NAD(+)--diphthamide ADP-ribosyltransferase], with EC number [2.4.2.36]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].

Reference

Crystal structure of nucleotide-free diphtheria toxin., Bell CE, Eisenberg D, Biochemistry. 1997 Jan 21;36(3):481-8. PMID:9012663

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