1h74

From Proteopedia

Revision as of 06:27, 30 October 2007

CRYSTAL STRUCTURE OF HOMOSERINE KINASE COMPLEXED WITH ILE

Overview

Homoserine kinase (HSK), the fourth enzyme in the aspartate pathway of, amino acid biosynthesis, catalyzes the phosphorylation of L-homoserine, (Hse) to L-homoserine phosphate, an intermediate in the production of, L-threonine, L-isoleucine, and in higher plants, L-methionine. The, high-resolution structures of Methanococcus jannaschii HSK ternary, complexes with its amino acid substrate and ATP analogues have been, determined by X-ray crystallography. These structures reveal the, structural determinants of the tight and highly specific binding of Hse, which is coupled with local conformational changes that enforce the, sequestration of the substrate. The delta-hydroxyl group of bound Hse is, only 3.4 A away from the gamma-phosphate of the bound nucleotide, poised, for the in-line attack ... [(full description)]

About this Structure

1H74 is a [Single protein] structure of sequence from [Methanococcus jannaschii] with MG, ILE, ADP and SAP as [ligands]. Active as [Transferase], with EC number [2.7.1.39]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structural basis for the catalysis and substrate specificity of homoserine kinase., Krishna SS, Zhou T, Daugherty M, Osterman A, Zhang H, Biochemistry. 2001 Sep 11;40(36):10810-8. PMID:11535056

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