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1jud

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[[Image:1jud.jpg|left|200px]]
 
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{{Structure
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==L-2-HALOACID DEHALOGENASE==
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|PDB= 1jud |SIZE=350|CAPTION= <scene name='initialview01'>1jud</scene>, resolution 2.5&Aring;
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<StructureSection load='1jud' size='340' side='right'caption='[[1jud]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE= <scene name='pdbsite=CAT:Mutagenesis+Experiments+Have+Shown+That+These+Nine+Resid+...'>CAT</scene>
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1jud]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._YL Pseudomonas sp. YL]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JUD FirstGlance]. <br>
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|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]
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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|GENE= L-DEX YL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=286 Pseudomonas])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jud OCA], [https://pdbe.org/1jud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jud RCSB], [https://www.ebi.ac.uk/pdbsum/1jud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jud ProSAT]</span></td></tr>
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}}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/HAD_PSEUY HAD_PSEUY] Catalyzes the hydrolytic dehalogenation of small (S)-2-haloalkanoic acids to yield the corresponding (R)-2-hydroxyalkanoic acids. Acts on acids of short chain lengths, C(2) to C(4), with inversion of configuration at C-2.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ju/1jud_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jud ConSurf].
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<div style="clear:both"></div>
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'''L-2-HALOACID DEHALOGENASE'''
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==See Also==
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*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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.
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[[Category: Large Structures]]
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[[Category: Pseudomonas sp. YL]]
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==About this Structure==
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[[Category: Esaki N]]
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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].
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[[Category: Fujii T]]
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[[Category: Hata Y]]
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==Reference==
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[[Category: Hisano T]]
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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]
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[[Category: Kurihara T]]
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[[Category: (S)-2-haloacid dehalogenase]]
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[[Category: Liu J-Q]]
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[[Category: Pseudomonas]]
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[[Category: Soda K]]
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[[Category: Single protein]]
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[[Category: Esaki, N.]]
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[[Category: Fujii, T.]]
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[[Category: Hata, Y.]]
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[[Category: Hisano, T.]]
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[[Category: Kurihara, T.]]
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[[Category: Liu, J Q.]]
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[[Category: Soda, K.]]
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[[Category: dehalogenase]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:08:37 2008''
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Current revision

L-2-HALOACID DEHALOGENASE

PDB ID 1jud

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