2pll

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==Overview==
==Overview==
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Arginase is a manganese metalloenzyme that catalyzes the hydrolysis of, l-arginine to yield l-ornithine and urea. In order to establish a, foundation for future neutron diffraction studies that will provide, conclusive structural information regarding proton/deuteron positions in, enzyme-inhibitor complexes, we have expressed, purified, assayed, and, determined the X-ray crystal structure of perdeuterated (i.e., fully, deuterated) human arginase I complexed with 2(S)-amino-6-boronohexanoic, acid (ABH) at 1.90A resolution. Prior to the neutron diffraction, experiment, it is important to establish that perdeuteration does not, cause any unanticipated structural or functional changes. Accordingly, we, find that perdeuterated human arginase I exhibits catalytic activity, essentially identical to that of the unlabeled enzyme. Additionally, the, structure of the perdeuterated human arginase I-ABH complex is identical, to that of the corresponding complex with the unlabeled enzyme. Therefore, we conclude that crystals of the perdeuterated human arginase I-ABH, complex are suitable for neutron crystallographic study.
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Arginase is a manganese metalloenzyme that catalyzes the hydrolysis of l-arginine to yield l-ornithine and urea. In order to establish a foundation for future neutron diffraction studies that will provide conclusive structural information regarding proton/deuteron positions in enzyme-inhibitor complexes, we have expressed, purified, assayed, and determined the X-ray crystal structure of perdeuterated (i.e., fully deuterated) human arginase I complexed with 2(S)-amino-6-boronohexanoic acid (ABH) at 1.90A resolution. Prior to the neutron diffraction experiment, it is important to establish that perdeuteration does not cause any unanticipated structural or functional changes. Accordingly, we find that perdeuterated human arginase I exhibits catalytic activity essentially identical to that of the unlabeled enzyme. Additionally, the structure of the perdeuterated human arginase I-ABH complex is identical to that of the corresponding complex with the unlabeled enzyme. Therefore, we conclude that crystals of the perdeuterated human arginase I-ABH complex are suitable for neutron crystallographic study.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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Expression, purification, assay, and crystal structure of perdeuterated human arginase I., Di Costanzo L, Moulin M, Haertlein M, Meilleur F, Christianson DW, Arch Biochem Biophys. 2007 May 21;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17562323 17562323]
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Expression, purification, assay, and crystal structure of perdeuterated human arginase I., Di Costanzo L, Moulin M, Haertlein M, Meilleur F, Christianson DW, Arch Biochem Biophys. 2007 Sep 1;465(1):82-9. Epub 2007 May 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17562323 17562323]
[[Category: Arginase]]
[[Category: Arginase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Christianson, D.W.]]
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[[Category: Christianson, D W.]]
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[[Category: Costanzo, L.Di.]]
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[[Category: Costanzo, L Di.]]
[[Category: Haertlein, M.]]
[[Category: Haertlein, M.]]
[[Category: Meilleur, F.]]
[[Category: Meilleur, F.]]
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[[Category: perdeuterated protein; x-ray structure]]
[[Category: perdeuterated protein; x-ray structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:04:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:30:49 2008''

Revision as of 16:30, 21 February 2008


2pll, resolution 1.90Å

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Crystal structure of perdeuterated human arginase I

Overview

Arginase is a manganese metalloenzyme that catalyzes the hydrolysis of l-arginine to yield l-ornithine and urea. In order to establish a foundation for future neutron diffraction studies that will provide conclusive structural information regarding proton/deuteron positions in enzyme-inhibitor complexes, we have expressed, purified, assayed, and determined the X-ray crystal structure of perdeuterated (i.e., fully deuterated) human arginase I complexed with 2(S)-amino-6-boronohexanoic acid (ABH) at 1.90A resolution. Prior to the neutron diffraction experiment, it is important to establish that perdeuteration does not cause any unanticipated structural or functional changes. Accordingly, we find that perdeuterated human arginase I exhibits catalytic activity essentially identical to that of the unlabeled enzyme. Additionally, the structure of the perdeuterated human arginase I-ABH complex is identical to that of the corresponding complex with the unlabeled enzyme. Therefore, we conclude that crystals of the perdeuterated human arginase I-ABH complex are suitable for neutron crystallographic study.

About this Structure

2PLL is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Arginase, with EC number 3.5.3.1 Full crystallographic information is available from OCA.

Reference

Expression, purification, assay, and crystal structure of perdeuterated human arginase I., Di Costanzo L, Moulin M, Haertlein M, Meilleur F, Christianson DW, Arch Biochem Biophys. 2007 Sep 1;465(1):82-9. Epub 2007 May 21. PMID:17562323

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