2cst
From Proteopedia
(New page: 200px<br /><applet load="2cst" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cst, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:2cst.gif|left|200px]]<br /><applet load="2cst" size=" | + | [[Image:2cst.gif|left|200px]]<br /><applet load="2cst" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2cst, resolution 1.9Å" /> | caption="2cst, resolution 1.9Å" /> | ||
'''CRYSTAL STRUCTURE OF THE CLOSED FORM OF CHICKEN CYTOSOLIC ASPARTATE AMINOTRANSFERASE AT 1.9 ANGSTROMS RESOLUTION'''<br /> | '''CRYSTAL STRUCTURE OF THE CLOSED FORM OF CHICKEN CYTOSOLIC ASPARTATE AMINOTRANSFERASE AT 1.9 ANGSTROMS RESOLUTION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of chicken cytosolic aspartate aminotransferase | + | The crystal structure of chicken cytosolic aspartate aminotransferase (cAATase; EC 2.6.1.1) has been solved and refined at 1.9 A resolution. Orthorhombic crystals, space group P2(1)2(1)2(1), a = 56.4 A, b = 126.0 A and c = 142.3 A, were grown from polyethylene glycol solutions in the presence of maleate, a dicarboxylic inhibitor that forms a Michaelis-like complex. The pyridoxal form of the enzyme was used for crystallization. Diffraction data were collected using synchrotron radiation. The structure of the new orthorhombic crystal form was solved by molecular replacement using the partially refined 2.8 A resolution structure of the high-salt crystal form as a search model. The final value of the crystallographic R-factor after rigid body and restrained least-squares refinement is 0.175 with very good model geometry. The two 2-fold-related subunits of cAATase have distinct environments in the crystal lattice. Domain movement is strictly hindered by the lattice contacts in one subunit, while the second one possesses conformational freedom. Despite their different environments, both subunits were found in the closed conformation with one maleate molecule tightly bound in each active site. The present study allows a detailed comparison of the highly refined structures of the aspartate aminotransferase isozymes, and thus provide better insight into the role of conserved and variable residues in substrate recognition and catalysis. |
==About this Structure== | ==About this Structure== | ||
| - | 2CST is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with PLP and MAE as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] Full crystallographic information is available from [http:// | + | 2CST is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] with <scene name='pdbligand=PLP:'>PLP</scene> and <scene name='pdbligand=MAE:'>MAE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Aspartate_transaminase Aspartate transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.1 2.6.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CST OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Borisov, V | + | [[Category: Borisov, V V.]] |
| - | [[Category: Malashkevich, V | + | [[Category: Malashkevich, V N.]] |
| - | [[Category: Strokopytov, B | + | [[Category: Strokopytov, B V.]] |
[[Category: MAE]] | [[Category: MAE]] | ||
[[Category: PLP]] | [[Category: PLP]] | ||
[[Category: transferase(aminotransferase)]] | [[Category: transferase(aminotransferase)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:52:02 2008'' |
Revision as of 14:52, 21 February 2008
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CRYSTAL STRUCTURE OF THE CLOSED FORM OF CHICKEN CYTOSOLIC ASPARTATE AMINOTRANSFERASE AT 1.9 ANGSTROMS RESOLUTION
Overview
The crystal structure of chicken cytosolic aspartate aminotransferase (cAATase; EC 2.6.1.1) has been solved and refined at 1.9 A resolution. Orthorhombic crystals, space group P2(1)2(1)2(1), a = 56.4 A, b = 126.0 A and c = 142.3 A, were grown from polyethylene glycol solutions in the presence of maleate, a dicarboxylic inhibitor that forms a Michaelis-like complex. The pyridoxal form of the enzyme was used for crystallization. Diffraction data were collected using synchrotron radiation. The structure of the new orthorhombic crystal form was solved by molecular replacement using the partially refined 2.8 A resolution structure of the high-salt crystal form as a search model. The final value of the crystallographic R-factor after rigid body and restrained least-squares refinement is 0.175 with very good model geometry. The two 2-fold-related subunits of cAATase have distinct environments in the crystal lattice. Domain movement is strictly hindered by the lattice contacts in one subunit, while the second one possesses conformational freedom. Despite their different environments, both subunits were found in the closed conformation with one maleate molecule tightly bound in each active site. The present study allows a detailed comparison of the highly refined structures of the aspartate aminotransferase isozymes, and thus provide better insight into the role of conserved and variable residues in substrate recognition and catalysis.
About this Structure
2CST is a Single protein structure of sequence from Gallus gallus with and as ligands. Active as Aspartate transaminase, with EC number 2.6.1.1 Full crystallographic information is available from OCA.
Reference
Crystal structure of the closed form of chicken cytosolic aspartate aminotransferase at 1.9 A resolution., Malashkevich VN, Strokopytov BV, Borisov VV, Dauter Z, Wilson KS, Torchinsky YM, J Mol Biol. 1995 Mar 17;247(1):111-24. PMID:7897655
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