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[[Image:1jud.jpg|left|200px]]<br /><applet load="1jud" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jud, resolution 2.5&Aring;" />
'''L-2-HALOACID DEHALOGENASE'''<br />


==Overview==
==L-2-HALOACID DEHALOGENASE==
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.
<StructureSection load='1jud' size='340' side='right'caption='[[1jud]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
</table>
== Function ==
[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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ju/1jud_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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].
*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=8702766 8702766]
[[Category: Large Structures]]
[[Category: (S)-2-haloacid dehalogenase]]
[[Category: Pseudomonas sp. YL]]
[[Category: Pseudomonas]]
[[Category: Esaki N]]
[[Category: Single protein]]
[[Category: Fujii T]]
[[Category: Esaki, N.]]
[[Category: Hata Y]]
[[Category: Fujii, T.]]
[[Category: Hisano T]]
[[Category: Hata, Y.]]
[[Category: Kurihara T]]
[[Category: Hisano, T.]]
[[Category: Liu J-Q]]
[[Category: Kurihara, T.]]
[[Category: Soda K]]
[[Category: Liu, J.Q.]]
[[Category: Soda, K.]]
[[Category: dehalogenase]]
[[Category: hydrolase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 16:38:42 2007''

Latest revision as of 10:42, 7 February 2024

L-2-HALOACID DEHALOGENASEL-2-HALOACID DEHALOGENASE

Structural highlights

1jud is a 1 chain structure with sequence from Pseudomonas sp. YL. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1jud, resolution 2.50Å

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