1kq7
From Proteopedia
(New page: 200px<br /><applet load="1kq7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kq7, resolution 2.60Å" /> '''E315Q Mutant Form of...) |
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| - | [[Image:1kq7.jpg|left|200px]]<br /><applet load="1kq7" size=" | + | [[Image:1kq7.jpg|left|200px]]<br /><applet load="1kq7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1kq7, resolution 2.60Å" /> | caption="1kq7, resolution 2.60Å" /> | ||
'''E315Q Mutant Form of Fumarase C from E.coli'''<br /> | '''E315Q Mutant Form of Fumarase C from E.coli'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Fumarase catalyzes the reversible conversion of fumarate to S- malate | + | Fumarase catalyzes the reversible conversion of fumarate to S- malate during the operation of the ubiquitous Kreb's cycle. Previous studies have shown that the active site includes side chains from three of the four subunits within the tetrameric enzyme. We used a clinically observed human mutation to narrow our search for potential catalytic groups within the fumarase active site. Offspring homozygous for the missense mutation, a G-955-C transversion in the fumarase gene, results in the substitution of a glutamine at amino acid 319 for the normal glutamic acid. To more fully understand the implications of this mutation, a single-step site-directed mutagenesis method was used to generate the homologous substitution at position 315 within fumarase C from Escherichia coli. Subsequent kinetic and X-ray crystal structure analyses show changes in the turnover number and the cocrystal structure with bound citrate. |
==About this Structure== | ==About this Structure== | ||
| - | 1KQ7 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 MLT and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http:// | + | 1KQ7 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 <scene name='pdbligand=MLT:'>MLT</scene> and <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQ7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Skarda, J.]] | [[Category: Skarda, J.]] | ||
[[Category: Spencer, J.]] | [[Category: Spencer, J.]] | ||
| - | [[Category: Weaver, T | + | [[Category: Weaver, T M.]] |
[[Category: CIT]] | [[Category: CIT]] | ||
[[Category: MLT]] | [[Category: MLT]] | ||
[[Category: fumarate lyase]] | [[Category: fumarate lyase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:50 2008'' |
Revision as of 11:36, 21 February 2008
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E315Q Mutant Form of Fumarase C from E.coli
Overview
Fumarase catalyzes the reversible conversion of fumarate to S- malate during the operation of the ubiquitous Kreb's cycle. Previous studies have shown that the active site includes side chains from three of the four subunits within the tetrameric enzyme. We used a clinically observed human mutation to narrow our search for potential catalytic groups within the fumarase active site. Offspring homozygous for the missense mutation, a G-955-C transversion in the fumarase gene, results in the substitution of a glutamine at amino acid 319 for the normal glutamic acid. To more fully understand the implications of this mutation, a single-step site-directed mutagenesis method was used to generate the homologous substitution at position 315 within fumarase C from Escherichia coli. Subsequent kinetic and X-ray crystal structure analyses show changes in the turnover number and the cocrystal structure with bound citrate.
About this Structure
1KQ7 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Fumarate hydratase, with EC number 4.2.1.2 Full crystallographic information is available from OCA.
Reference
X-ray crystallographic and kinetic correlation of a clinically observed human fumarase mutation., Estevez M, Skarda J, Spencer J, Banaszak L, Weaver TM, Protein Sci. 2002 Jun;11(6):1552-7. PMID:12021453
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