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[[Image:1zmt.gif|left|200px]]


{{Structure
==Structure of haloalcohol dehalogenase HheC of Agrobacterium radiobacter AD1 in complex with (R)-para-nitro styrene oxide, with a water molecule in the halide-binding site==
|PDB= 1zmt |SIZE=350|CAPTION= <scene name='initialview01'>1zmt</scene>, resolution 1.70&Aring;
<StructureSection load='1zmt' size='340' side='right'caption='[[1zmt]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=RNO:(R)-PARA-NITROSTYRENE OXIDE'>RNO</scene>
<table><tr><td colspan='2'>[[1zmt]] 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=1ZMT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZMT FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RNO:(R)-PARA-NITROSTYRENE+OXIDE'>RNO</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=1zmt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zmt OCA], [https://pdbe.org/1zmt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zmt RCSB], [https://www.ebi.ac.uk/pdbsum/1zmt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zmt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q93D82_RHIRD Q93D82_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/zm/1zmt_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=1zmt ConSurf].
<div style="clear:both"></div>


'''Structure of haloalcohol dehalogenase HheC of Agrobacterium radiobacter AD1 in complex with (R)-para-nitro styrene oxide, with a water molecule in the halide-binding site'''
==See Also==
 
*[[Dehalogenase 3D structures|Dehalogenase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Halo alcohol dehalogenase HheC catalyzes the highly enantioselective dehalogenation of vicinal halo alcohols to epoxides, as well as the reverse reaction, the enantioselective and beta-regioselective nucleophilic ring opening of epoxides by pseudo-halides such as azide and cyanide. To investigate this latter reaction, we determined X-ray structures of complexes of HheC with the favored and unfavored enantiomers of para-nitrostyrene oxide. The aromatic parts of the two enantiomers bind in a very similar way, but the epoxide ring of the unfavored (S)-enantiomer binds in a nonproductive inverted manner, with the epoxide oxygen and Cbeta atom positions interchanged with respect to those of the favored (R)-enantiomer. The calculated difference in relative Gibbs binding energy is in agreement with the observed loss of a single hydrogen bond in the S bound state with respect to the R bound state. Our results indicate that it is the nonproductive binding of the unfavored (S)-enantiomer, rather than the difference in affinity for the two enantiomers, that allows HheC to catalyze the azide-mediated ring opening of para-nitrostyrene oxide with high enantioselectivity. This work represents a rare opportunity to explain the enantioselectivity of an enzymatic reaction by comparison of crystallographic data on the binding of both the favored and unfavored enantiomers.
 
==About this Structure==
1ZMT 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=1ZMT OCA].
 
==Reference==
Structural basis for the enantioselectivity of an epoxide ring opening reaction catalyzed by halo alcohol dehalogenase HheC., de Jong RM, Tiesinga JJ, Villa A, Tang L, Janssen DB, Dijkstra BW, J Am Chem Soc. 2005 Sep 28;127(38):13338-43. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16173767 16173767]
[[Category: Agrobacterium tumefaciens]]
[[Category: Agrobacterium tumefaciens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dijkstra, B W.]]
[[Category: Dijkstra BW]]
[[Category: Janssen, D B.]]
[[Category: Janssen DB]]
[[Category: Jong, R M.de.]]
[[Category: Tang L]]
[[Category: Tang, L.]]
[[Category: Tiesinga JJW]]
[[Category: Tiesinga, J J.W.]]
[[Category: Villa A]]
[[Category: Villa, A.]]
[[Category: De Jong RM]]
[[Category: RNO]]
[[Category: enantioselectivity]]
[[Category: epoxide catalysis]]
[[Category: haloalcohol dehalogenase]]
[[Category: halohydrin dehalogenase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:37:26 2008''

Latest revision as of 12:05, 14 February 2024

Structure of haloalcohol dehalogenase HheC of Agrobacterium radiobacter AD1 in complex with (R)-para-nitro styrene oxide, with a water molecule in the halide-binding siteStructure of haloalcohol dehalogenase HheC of Agrobacterium radiobacter AD1 in complex with (R)-para-nitro styrene oxide, with a water molecule in the halide-binding site

Structural highlights

1zmt is a 4 chain structure with sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q93D82_RHIRD

Evolutionary Conservation

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

See Also

1zmt, resolution 1.70Å

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