2fus

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(New page: 200px<br /> <applet load="2fus" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fus, resolution 2.2&Aring;" /> '''MUTATIONS OF FUMARAS...)
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==About this Structure==
==About this Structure==
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2FUS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with CIT as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.2 4.2.1.2]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FUS OCA]].
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2FUS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with CIT as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Fumarate_hydratase Fumarate hydratase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.2 4.2.1.2]]. Structure known Active Site: S1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FUS OCA]].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9098893 9098893]
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9098893 9098893]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Fumarate hydratase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Banaszak, L.J.]]
[[Category: Banaszak, L.J.]]
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[[Category: kreb's cycle enzyme]]
[[Category: kreb's cycle enzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 20:59:27 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:43:29 2007''

Revision as of 11:38, 30 October 2007


2fus, resolution 2.2Å

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MUTATIONS OF FUMARASE THAT DISTINGUISH BETWEEN THE ACTIVE SITE AND A NEARBY DICARBOXYLIC ACID BINDING 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

2FUS is a [Single protein] structure of sequence from [Escherichia coli] with CIT as [ligand]. Active as [Fumarate hydratase], with EC number [4.2.1.2]. Structure known Active Site: S1. 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 Tue Oct 30 13:43:29 2007

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