1jud
From Proteopedia
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| - | [[Image:1jud.jpg|left|200px]] | + | [[Image:1jud.jpg|left|200px]] |
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| - | '''L-2-HALOACID DEHALOGENASE''' | + | {{Structure |
| + | |PDB= 1jud |SIZE=350|CAPTION= <scene name='initialview01'>1jud</scene>, resolution 2.5Å | ||
| + | |SITE= <scene name='pdbsite=CAT:Mutagenesis+Experiments+Have+Shown+That+These+Nine+Resid+...'>CAT</scene> | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= L-DEX YL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=286 Pseudomonas]) | ||
| + | }} | ||
| + | |||
| + | '''L-2-HALOACID DEHALOGENASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JUD is a [ | + | 1JUD is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas Pseudomonas]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JUD OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8702766 8702766] |
[[Category: (S)-2-haloacid dehalogenase]] | [[Category: (S)-2-haloacid dehalogenase]] | ||
[[Category: Pseudomonas]] | [[Category: Pseudomonas]] | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:08:37 2008'' |
Revision as of 10:08, 20 March 2008
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| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Gene: | L-DEX YL (Pseudomonas) | ||||||
| Activity: | (S)-2-haloacid dehalogenase, with EC number 3.8.1.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
L-2-HALOACID DEHALOGENASE
Overview
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 Structure
1JUD is a Single protein structure of sequence from Pseudomonas. Full crystallographic information is available from OCA.
Reference
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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