1yfm
From Proteopedia
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| - | [[Image:1yfm. | + | [[Image:1yfm.jpg|left|200px]]<br /><applet load="1yfm" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1yfm" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1yfm, resolution 2.6Å" /> | caption="1yfm, resolution 2.6Å" /> | ||
'''RECOMBINANT YEAST FUMARASE'''<br /> | '''RECOMBINANT YEAST FUMARASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YFM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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] | + | 1YFM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. 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] Known structural/functional Site: <scene name='pdbsite=AVE:Multi-Subunit Active Site Of Fumarase. H213, T126 S124, ...'>AVE</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YFM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: multi-subunit active site]] | [[Category: multi-subunit active site]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:41:18 2007'' |
Revision as of 16:31, 18 December 2007
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RECOMBINANT YEAST FUMARASE
Overview
Crystal structures for both native and recombinant forms of yeast fumarase, from Saccharomyces cerevisiae have been completed to moderate resolution, by two separate laboratories. The recombinant form was obtained by the, construction of an expression plasmid for Escherichia coli. Despite a high, level of amino acid sequence similarity, purification of the eukaryotic, enzyme from the wild-type prokaryotic enzyme was feasible. The crystal, structure of the native form, NY-fumarase, encompasses residues R22, through M484, while the recombinant form, RY-fumarase, consists of, residues S27 through L485. Both crystal structures lack the N-terminal, translocation segment. Each subunit of the homo-tetrameric protein has, three domains. The active site is formed by segments from each of three, polypeptide chains. The results of these studies on the eukaryotic, proteins are unique, since the recombinant form was done in the absence of, dicarboxylic acid and has an unoccupied active site. As a comparison, native fumarase was crystallized in the presence of the competitive, inhibitor, meso-tartrate. Meso-tartrate occupies a position close to that, of the bound citrate molecule found in the active site of the E. coli, enzyme. This inhibitor participates in hydrogen bonding to an active-site, water molecule. The independent determination of the two structures, provides further evidence that an active-site water molecule may play an, active role in the fumarase-catalyzed reaction.
About this Structure
1YFM is a Single protein structure of sequence from Saccharomyces cerevisiae. Active as Fumarate hydratase, with EC number 4.2.1.2 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structures of native and recombinant yeast fumarase., Weaver T, Lees M, Zaitsev V, Zaitseva I, Duke E, Lindley P, McSweeny S, Svensson A, Keruchenko J, Keruchenko I, Gladilin K, Banaszak L, J Mol Biol. 1998 Jul 17;280(3):431-42. PMID:9665847
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