1umy
From Proteopedia
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Revision as of 14:01, 30 October 2007
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BHMT FROM RAT LIVER
Overview
Betaine homocysteine S-methyltransferase (BHMT) is one of the two enzymes, known to methylate homocysteine to generate methionine in the liver. It, presents a Zn(2+) atom linked to three essential Cys residues. The crystal, structure of rat liver BHMT has been solved at 2.5A resolution, using, crystals with P2(1) symmetry and 45% solvent content in the cell. The, asymmetric unit contains the whole functional tetramer showing point, symmetry 222. The overall fold of the subunit consists mostly of a, (alpha/beta)(8) barrel, as for human BHMT. From the end of the barrel, the, polypeptide chain extends away and makes many interactions with a, different subunit, forming tight dimers. The most remarkable structural, feature of rat liver BHMT is the presence of a helix including residues, ... [(full description)]
About this Structure
1UMY is a [Single protein] structure of sequence from [[1]] with ZN and BME as [ligands]. Active as [Betaine--homocysteine S-methyltransferase], with EC number [2.1.1.5]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of rat liver betaine homocysteine s-methyltransferase reveals new oligomerization features and conformational changes upon substrate binding., Gonzalez B, Pajares MA, Martinez-Ripoll M, Blundell TL, Sanz-Aparicio J, J Mol Biol. 2004 May 7;338(4):771-82. PMID:15099744
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