1xgn

From Proteopedia

Revision as of 14:27, 30 October 2007

METHIONINE AMINOPEPTIDASE FROM HYPERTHERMOPHILE PYROCOCCUS FURIOSUS

Overview

The structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus (PfMAP) with an optimal growth temperature of 100, degreesC was determined by the multiple isomorphous replacement method and, refined in three different crystal forms, one monoclinic and two, hexagonal, at resolutions of 2.8, 2.9, and 3.5 A. The resolution of the, monoclinic crystal form was extended to 1.75 A by water-mediated, transformation to a low-humidity form, and the obtained diffraction data, used for high-resolution structure refinement. This is the first, description of a eukaryotic type methionine aminopeptidase structure. The, PfMAP molecule is composed of two domains, a catalytic domain and an, insertion domain, connected via two antiparallel beta-strands. The, catalytic domain, which ... [(full description)]

About this Structure

1XGN is a [Single protein] structure of sequence from [Pyrococcus furiosus] with CO as [ligand]. Active as [Methionyl aminopeptidase], with EC number [3.4.11.18]. Structure known Active Sites: ACA and ACB. Full crystallographic information is available from [OCA].

Reference

Crystal structure of methionine aminopeptidase from hyperthermophile, Pyrococcus furiosus., Tahirov TH, Oki H, Tsukihara T, Ogasahara K, Yutani K, Ogata K, Izu Y, Tsunasawa S, Kato I, J Mol Biol. 1998 Nov 20;284(1):101-24. PMID:9811545

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