1lxy

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(New page: 200px<br /><applet load="1lxy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lxy, resolution 2.00&Aring;" /> '''Crystal Structure of...)
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caption="1lxy, resolution 2.00&Aring;" />
'''Crystal Structure of Arginine Deiminase covalently linked with L-citrulline'''<br />
'''Crystal Structure of Arginine Deiminase covalently linked with L-citrulline'''<br />
==Overview==
==Overview==
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Arginine deiminase (ADI), an enzyme that hydrolyzes arginine to generate, energy in many parasitic microorganisms, has potent anticancer activities, and can halt growth of solid tumors. We determined the crystal structure, of ADI from Mycoplasma arginini in two different forms (1.6 and 2.0 A, resolution) using multiple isomorphous replacement. ADI shares common, structural features with the arginine-catabolizing enzymes Arg:Gly, amidinotransferase and dimethylarginine dimethyl-aminohydrolase; ADI, contains an additional domain of five helices. The scissile C-N bonds of, the substrates and the catalytic triads (Cys398-His269-Glu213 of ADI) for, the three enzymes superimpose on each other. The ADI structure from form I, crystals corresponds to a tetrahedral intermediate with four heteroatoms, (1S, 2N, 1O) covalently bonded to the reaction-center carbon. The, structure from form II crystals represents an amidino-enzyme complex; the, reaction-center carbon is covalently bonded to Cys398 sulfur and two, nitrogens, and the reacting water molecule is only 2.54 A away.
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Arginine deiminase (ADI), an enzyme that hydrolyzes arginine to generate energy in many parasitic microorganisms, has potent anticancer activities and can halt growth of solid tumors. We determined the crystal structure of ADI from Mycoplasma arginini in two different forms (1.6 and 2.0 A resolution) using multiple isomorphous replacement. ADI shares common structural features with the arginine-catabolizing enzymes Arg:Gly amidinotransferase and dimethylarginine dimethyl-aminohydrolase; ADI contains an additional domain of five helices. The scissile C-N bonds of the substrates and the catalytic triads (Cys398-His269-Glu213 of ADI) for the three enzymes superimpose on each other. The ADI structure from form I crystals corresponds to a tetrahedral intermediate with four heteroatoms (1S, 2N, 1O) covalently bonded to the reaction-center carbon. The structure from form II crystals represents an amidino-enzyme complex; the reaction-center carbon is covalently bonded to Cys398 sulfur and two nitrogens, and the reacting water molecule is only 2.54 A away.
==About this Structure==
==About this Structure==
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1LXY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_arginini Mycoplasma arginini] with CIR and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arginine_deiminase Arginine deiminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.6 3.5.3.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LXY OCA].
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1LXY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycoplasma_arginini Mycoplasma arginini] with <scene name='pdbligand=CIR:'>CIR</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Arginine_deiminase Arginine deiminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.3.6 3.5.3.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LXY OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Arnold, E.]]
[[Category: Arnold, E.]]
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[[Category: Buttler, G.H.]]
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[[Category: Buttler, G H.]]
[[Category: Das, K.]]
[[Category: Das, K.]]
[[Category: Kwiatkowski, V.]]
[[Category: Kwiatkowski, V.]]
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[[Category: deiminase; hydrolase; 5-fold pseudo-symmetric domain; 5-helix bundle domain]]
[[Category: deiminase; hydrolase; 5-fold pseudo-symmetric domain; 5-helix bundle domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:58:11 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:49:29 2008''

Revision as of 11:49, 21 February 2008


1lxy, resolution 2.00Å

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Crystal Structure of Arginine Deiminase covalently linked with L-citrulline

Overview

Arginine deiminase (ADI), an enzyme that hydrolyzes arginine to generate energy in many parasitic microorganisms, has potent anticancer activities and can halt growth of solid tumors. We determined the crystal structure of ADI from Mycoplasma arginini in two different forms (1.6 and 2.0 A resolution) using multiple isomorphous replacement. ADI shares common structural features with the arginine-catabolizing enzymes Arg:Gly amidinotransferase and dimethylarginine dimethyl-aminohydrolase; ADI contains an additional domain of five helices. The scissile C-N bonds of the substrates and the catalytic triads (Cys398-His269-Glu213 of ADI) for the three enzymes superimpose on each other. The ADI structure from form I crystals corresponds to a tetrahedral intermediate with four heteroatoms (1S, 2N, 1O) covalently bonded to the reaction-center carbon. The structure from form II crystals represents an amidino-enzyme complex; the reaction-center carbon is covalently bonded to Cys398 sulfur and two nitrogens, and the reacting water molecule is only 2.54 A away.

About this Structure

1LXY is a Single protein structure of sequence from Mycoplasma arginini with and as ligands. Active as Arginine deiminase, with EC number 3.5.3.6 Full crystallographic information is available from OCA.

Reference

Crystal structures of arginine deiminase with covalent reaction intermediates; implications for catalytic mechanism., Das K, Butler GH, Kwiatkowski V, Clark AD Jr, Yadav P, Arnold E, Structure. 2004 Apr;12(4):657-67. PMID:15062088

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