2b0j: Difference between revisions

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[[Image:2b0j.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_2b0j|  PDB=2b0j  |  SCENE=  }}  
{{STRUCTURE_2b0j|  PDB=2b0j  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_16540118}}


==About this Structure==
==About this Structure==
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[[Category: Helix bundle]]
[[Category: Helix bundle]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
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