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2b0j

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Image:2b0j.gif

2b0j, resolution 1.75Å

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The crystal structure of the apoenzyme of the iron-sulfur-cluster-free hydrogenase (Hmd)

Overview

The iron-sulphur cluster-free hydrogenase (Hmd, EC 1.12.98.2) from, methanogenic archaea is a novel type of hydrogenase that tightly binds an, iron-containing cofactor. The iron is coordinated by two CO molecules, one, sulphur and a pyridone derivative, which is linked via a phosphodiester, bond to a guanosine base. We report here on the crystal structure of the, Hmd apoenzyme from Methanocaldococcus jannaschii at 1.75 A and from, Methanopyrus kandleri at 2.4 A resolution. Homodimeric Hmd reveals a, unique architecture composed of one central and two identical peripheral, globular units. The central unit is composed of the intertwined C-terminal, segments of both subunits, forming a novel intersubunit fold. The two, peripheral units consist of the N-terminal domain of each subunit. The, Rossmann fold-like structure of the N-terminal domain contains a, mononucleotide-binding site, which could harbour the GMP moiety of the, cofactor. Another binding site for the iron-containing cofactor is most, probably Cys176, which is located at the bottom of a deep intersubunit, cleft and which has been shown to be essential for enzyme activity., Adjacent to the iron of the cofactor modelled as a ligand to Cys176, an, extended U-shaped extra electron density, interpreted as a, polyethyleneglycol fragment, suggests a binding site for the substrate, methenyltetrahydromethanopterin.

About this Structure

2B0J is a Single protein structure of sequence from Methanocaldococcus jannaschii. Active as 5,10-methenyltetrahydromethanopterin hydrogenase, with EC number 1.12.98.2 Full crystallographic information is available from OCA.

Reference

The crystal structure of the apoenzyme of the iron-sulphur cluster-free hydrogenase., Pilak O, Mamat B, Vogt S, Hagemeier CH, Thauer RK, Shima S, Vonrhein C, Warkentin E, Ermler U, J Mol Biol. 2006 May 5;358(3):798-809. Epub 2006 Mar 2. PMID:16540118

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