1qlh

From Proteopedia

Revision as of 13:56, 30 October 2007

HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NAD DOUBLE MUTANT OF GLY 293 ALA AND PRO 295 THR

Overview

When horse liver alcohol dehydrogenase binds coenzyme, a rotation of about, 10 degrees brings the catalytic domain closer to the coenzyme binding, domain and closes the active site cleft. The conformational change, requires that a flexible loop containing residues 293-298 in the coenzyme, binding domain rearranges so that the coenzyme and some amino acid, residues from the catalytic domain can be accommodated. The change appears, to control the rate of dissociation of the coenzyme and to be necessary, for installation of the proton relay system. In this study, directed, mutagenesis produced the activated Gly293Ala/Pro295Thr enzyme. X-ray, crystallography shows that the conformations of both free and complexed, forms of the mutated enzyme and wild-type apoenzyme are very similar., Binding ... [(full description)]

About this Structure

1QLH is a [Single protein] structure of sequence from [Equus caballus] with ZN and NAD as [ligands]. Active as [Alcohol dehydrogenase], with EC number [1.1.1.1]. Structure known Active Site: NAD. Full crystallographic information is available from [OCA].

Reference

Substitutions in a flexible loop of horse liver alcohol dehydrogenase hinder the conformational change and unmask hydrogen transfer., Ramaswamy S, Park DH, Plapp BV, Biochemistry. 1999 Oct 19;38(42):13951-9. PMID:10529241

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