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[[Image:1ehy.jpg|left|200px]]
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{{STRUCTURE_1ehy|  PDB=1ehy  |  SCENE=  }}
'''X-ray structure of the epoxide hydrolase from agrobacterium radiobacter ad1'''


==X-ray structure of the epoxide hydrolase from agrobacterium radiobacter ad1==
<StructureSection load='1ehy' size='340' side='right'caption='[[1ehy]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ehy]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EHY 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=1ehy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ehy OCA], [https://pdbe.org/1ehy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ehy RCSB], [https://www.ebi.ac.uk/pdbsum/1ehy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ehy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/O31243_RHIRD O31243_RHIRD]
== 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/eh/1ehy_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ehy ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Epoxide hydrolases catalyze the cofactor-independent hydrolysis of reactive and toxic epoxides. They play an essential role in the detoxification of various xenobiotics in higher organisms and in the bacterial degradation of several environmental pollutants. The first x-ray structure of one of these, from Agrobacterium radiobacter AD1, has been determined by isomorphous replacement at 2.1-A resolution. The enzyme shows a two-domain structure with the core having the alpha/beta hydrolase-fold topology. The catalytic residues, Asp107 and His275, are located in a predominantly hydrophobic environment between the two domains. A tunnel connects the back of the active-site cavity with the surface of the enzyme and provides access to the active site for the catalytic water molecule, which in the crystal structure, has been found at hydrogen bond distance to His275. Because of a crystallographic contact, the active site has become accessible for the Gln134 side chain, which occupies a position mimicking a bound substrate. The structure suggests Tyr152/Tyr215 as the residues involved in substrate binding, stabilization of the transition state, and possibly protonation of the epoxide oxygen.


==Overview==
The x-ray structure of epoxide hydrolase from Agrobacterium radiobacter AD1. An enzyme to detoxify harmful epoxides.,Nardini M, Ridder IS, Rozeboom HJ, Kalk KH, Rink R, Janssen DB, Dijkstra BW J Biol Chem. 1999 May 21;274(21):14579-86. PMID:10329649<ref>PMID:10329649</ref>
Epoxide hydrolases catalyze the cofactor-independent hydrolysis of reactive and toxic epoxides. They play an essential role in the detoxification of various xenobiotics in higher organisms and in the bacterial degradation of several environmental pollutants. The first x-ray structure of one of these, from Agrobacterium radiobacter AD1, has been determined by isomorphous replacement at 2.1-A resolution. The enzyme shows a two-domain structure with the core having the alpha/beta hydrolase-fold topology. The catalytic residues, Asp107 and His275, are located in a predominantly hydrophobic environment between the two domains. A tunnel connects the back of the active-site cavity with the surface of the enzyme and provides access to the active site for the catalytic water molecule, which in the crystal structure, has been found at hydrogen bond distance to His275. Because of a crystallographic contact, the active site has become accessible for the Gln134 side chain, which occupies a position mimicking a bound substrate. The structure suggests Tyr152/Tyr215 as the residues involved in substrate binding, stabilization of the transition state, and possibly protonation of the epoxide oxygen.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1EHY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Agrobacterium_tumefaciens Agrobacterium tumefaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EHY OCA].
</div>
<div class="pdbe-citations 1ehy" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
The x-ray structure of epoxide hydrolase from Agrobacterium radiobacter AD1. An enzyme to detoxify harmful epoxides., Nardini M, Ridder IS, Rozeboom HJ, Kalk KH, Rink R, Janssen DB, Dijkstra BW, J Biol Chem. 1999 May 21;274(21):14579-86. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10329649 10329649]
*[[Epoxide hydrolase 3D structures|Epoxide hydrolase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Agrobacterium tumefaciens]]
[[Category: Agrobacterium tumefaciens]]
[[Category: Microsomal epoxide hydrolase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Dijkstra BW]]
[[Category: Dijkstra, B W.]]
[[Category: Janssen DB]]
[[Category: Janssen, D B.]]
[[Category: Kalk KH]]
[[Category: Kalk, K H.]]
[[Category: Nardini M]]
[[Category: Nardini, M.]]
[[Category: Ridder IS]]
[[Category: Ridder, I S.]]
[[Category: Rink R]]
[[Category: Rink, R.]]
[[Category: Rozeboom HJ]]
[[Category: Rozeboom, H J.]]
[[Category: Alpha/beta hydrolase fold]]
[[Category: Epichlorohydrin]]
[[Category: Epoxide degradation]]
[[Category: Hydrolase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:07:14 2008''

Latest revision as of 06:34, 30 October 2024

X-ray structure of the epoxide hydrolase from agrobacterium radiobacter ad1

1ehy, resolution 2.10Å

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