1e5k
From Proteopedia
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[[Category: molybdopterin nucleotidyl-transferase]] | [[Category: molybdopterin nucleotidyl-transferase]] | ||
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Revision as of 13:01, 30 October 2007
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CRYSTAL STRUCTURE OF THE MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN MOBA (PROTEIN FA) FROM ESCHERICHIA COLI AT NEAR ATOMIC RESOLUTION
Overview
BACKGROUND: All mononuclear molybdoenzymes bind molybdenum in a complex, with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by, attachment of a GMP group to the terminal phosphate of molybdopterin to, form molybdopterin guanine dinucleotide (MGD). This modification reaction, is required for the functioning of many bacterial molybdoenzymes, including the nitrate reductases, dimethylsulfoxide (DMSO) and, trimethylamine-N-oxide (TMAO) reductases, and formate dehydrogenases. The, GMP attachment step is catalyzed by the cellular enzyme MobA. RESULTS: The, crystal structure of the 21.6 kDa E. coli MobA has been determined by MAD, phasing with selenomethionine-substituted protein and subsequently refined, at 1. ... [(full description)]
About this Structure
1E5K is a [Single protein] structure of sequence from [Escherichia coli] with LI and CIT as [ligands]. Structure known Active Sites: CI1 and CI2. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution., Stevenson CE, Sargent F, Buchanan G, Palmer T, Lawson DM, Structure. 2000 Nov 15;8(11):1115-25. PMID:11080634
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