1jud: Difference between revisions
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[[Image:1jud. | [[Image:1jud.jpg|left|200px]]<br /><applet load="1jud" size="450" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1jud, resolution 2.5Å" /> | caption="1jud, resolution 2.5Å" /> | ||
'''L-2-HALOACID DEHALOGENASE'''<br /> | '''L-2-HALOACID DEHALOGENASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1JUD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas Pseudomonas]. Active as [http://en.wikipedia.org/wiki/(S)-2-haloacid_dehalogenase (S)-2-haloacid dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.2 3.8.1.2] | 1JUD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas Pseudomonas]. Active as [http://en.wikipedia.org/wiki/(S)-2-haloacid_dehalogenase (S)-2-haloacid dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.2 3.8.1.2] Known structural/functional Site: <scene name='pdbsite=CAT:Mutagenesis Experiments Have Shown That These Nine Resid ...'>CAT</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JUD OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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Revision as of 17:28, 18 December 2007
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L-2-HALOACID DEHALOGENASE
OverviewOverview
L-2-Haloacid dehalogenase catalyzes the hydrolytic dehalogenation of, L-2-haloalkanoic acids to yield the corresponding D-2-hydroxyalkanoic, acids. The crystal structure of the homodimeric enzyme from Pseudomonas, sp. YL has been determined by a multiple isomorphous replacement method, and refined at 2.5 A resolution to a crystallographic R-factor of 19.5%., The subunit consists of two structurally distinct domains: the core domain, and the subdomain. The core domain has an alpha/beta structure formed by a, six-stranded parallel beta-sheet flanked by five alpha-helices. The, subdomain inserted into the core domain has a four helix bundle structure, providing the greater part of the interface for dimer formation. There is, an active site cavity between the domains. An experimentally identified, nucleophilic residue, Asp-10, is located on a loop following the, amino-terminal beta-strand in the core domain, and other functional, residues, Thr-14, Arg-41, Ser-118, Lys-151, Tyr-157, Ser-175, Asn-177, and, Asp-180, detected by a site-directed mutagenesis experiment, are arranged, around the nucleophile in the active site. Although the enzyme is an, alpha/beta-type hydrolase, it does not belong to the alpha/beta hydrolase, fold family, from the viewpoint of the topological feature and the, position of the nucleophile.
About this StructureAbout this Structure
1JUD is a Single protein structure of sequence from Pseudomonas. Active as (S)-2-haloacid dehalogenase, with EC number 3.8.1.2 Known structural/functional Site: . Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of L-2-haloacid dehalogenase from Pseudomonas sp. YL. An alpha/beta hydrolase structure that is different from the alpha/beta hydrolase fold., Hisano T, Hata Y, Fujii T, Liu JQ, Kurihara T, Esaki N, Soda K, J Biol Chem. 1996 Aug 23;271(34):20322-30. PMID:8702766
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