1l3c
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(New page: 200px<br /><applet load="1l3c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l3c, resolution 2.31Å" /> '''MT0146, THE PRECORRI...)
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Revision as of 18:05, 20 November 2007
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MT0146, THE PRECORRIN-6Y METHYLTRANSFERASE (CBIT) HOMOLOG FROM M. THERMOAUTOTROPHICUM, C2 SPACEGROUP WITH SHORT CELL
Overview
The CbiT and CbiE enzymes participate in the biosynthesis of vitamin B12., They are fused together in some organisms to form a protein called CobL, which catalyzes two methylations and one decarboxylation on a precorrin, intermediate. Because CbiE has sequence homology to canonical precorrin, methyltransferases, CbiT was hypothesized to catalyze the decarboxylation., We herein present the crystal structure of MT0146, the CbiT homolog from, Methanobacterium thermoautotrophicum. The protein shows structural, similarity to Rossmann-like S-adenosyl-methionine-dependent, methyltransferases, and our 1.9 A cocrystal structure shows that it binds, S-adenosyl-methionine in standard geometry near a binding pocket that, could accommodate a precorrin substrate. Therefore, MT0146/CbiT probably, functions as a precorrin methyltransferase and represents the first enzyme, identified with this activity that does not have the canonical precorrin, methyltransferase fold.
About this Structure
1L3C is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.
Reference
The crystal structure of MT0146/CbiT suggests that the putative precorrin-8w decarboxylase is a methyltransferase., Keller JP, Smith PM, Benach J, Christendat D, deTitta GT, Hunt JF, Structure. 2002 Nov;10(11):1475-87. PMID:12429089
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