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1fur
From Proteopedia
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(New page: 200px<br /> <applet load="1fur" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fur, resolution 1.95Å" /> '''FUMARASE MUTANT H18...)
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Revision as of 18:54, 29 October 2007
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FUMARASE MUTANT H188N WITH BOUND SUBSTRATE L-MALATE AT PUTATIVE ACTIVATOR SITE
Overview
Two mutant forms of fumarase C from E. coli have been made using PCR and, recombinant DNA. The recombinant form of the protein included a histidine, arm on the C-terminal facilitating purification. Based on earlier studies, two different carboxylic acid binding sites, labeled A- and B-, were, observed in crystal structures of the wild type and inhibited forms of the, enzyme. A histidine at each of the sites was mutated to an asparagine., H188N at the A-site resulted in a large decrease in specific activity, while the H129N mutation at the B-site had essentially no effect. From the, results, we conclude that the A-site is indeed the active site, and a dual, role for H188 as a potential catalytic base is proposed. Crystal, structures of the two mutant proteins produced some unexpected ... [(full description)]
About this Structure
1FUR is a [Single protein] structure of sequence from [Escherichia coli] with MLT as [ligand]. Active as [[1]], with EC number [4.2.1.2]. Full crystallographic information is available from [OCA].
Reference
Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site., Weaver T, Lees M, Banaszak L, Protein Sci. 1997 Apr;6(4):834-42. PMID:9098893
Page seeded by OCA on Mon Oct 29 20:59:23 2007
