1zo8: Difference between revisions

Line 1:

[[Image:~~1zo8~~.~~png~~|~~left~~|~~200px~~]]

==X-ray Structure of the haloalcohol dehalogenase HheC of Agrobacterium radiobacter AD1 in complex with (S)-para-nitrostyrene oxide, with a water molecule in the halide-binding site==

== Structural highlights ==

<table><tr><td colspan='2'>[[1zo8]] is a 16 chain structure with 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=1ZO8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZO8 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SNO:(S)-PARA-NITROSTYRENE+OXIDE'>SNO</scene><br>

<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zmo|1zmo]], [[1zmt|1zmt]]</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zo8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zo8 RCSB], [http://www.ebi.ac.uk/pdbsum/1zo8 PDBsum]</span></td></tr>

<table>

== Evolutionary Conservation ==

[[Image:Consurf_key_small.gif|200px|right]]

Check<jmol>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zo/1zo8_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/chain_selection.php?pdb_ID=2ata ConSurf].

== Publication Abstract from PubMed ==

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.

~~{{STRUCTURE_1zo8| PDB=1zo8 | SCENE= }}~~

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:16173767<ref>PMID:16173767</ref>

~~===X-ray Structure~~ of the ~~haloalcohol dehalogenase HheC~~ of ~~Agrobacterium radiobacter AD1 in complex with (S)-para-nitrostyrene oxide, with a water molecule in the halide-binding site===~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

~~{{ABSTRACT_PUBMED_16173767}}~~

==See Also==

*[[Dehalogenase|Dehalogenase]]

==~~About this Structure~~==

== References ==

[[~~1zo8]] is a 16 chain structure with 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=1ZO8 OCA~~].

__TOC__

==~~Reference~~==

</StructureSection>

<~~ref group="xtra">PMID:016173767<~~/~~ref~~><~~references group="xtra"~~/>

[[Category: Agrobacterium tumefaciens]]

[[Category: Dijkstra, B W.]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-[[Image:1zo8.png|left|200px]]
+==X-ray Structure of the haloalcohol dehalogenase HheC of Agrobacterium radiobacter AD1 in complex with (S)-para-nitrostyrene oxide, with a water molecule in the halide-binding site==
+<StructureSection load='1zo8' size='340' side='right' caption='[[1zo8]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1zo8]] is a 16 chain structure with 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=1ZO8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZO8 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SNO:(S)-PARA-NITROSTYRENE+OXIDE'>SNO</scene><br>
+<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zmo|1zmo]], [[1zmt|1zmt]]</td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zo8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zo8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1zo8 RCSB], [http://www.ebi.ac.uk/pdbsum/1zo8 PDBsum]</span></td></tr>
+<table>
+== 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/zo/1zo8_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/chain_selection.php?pdb_ID=2ata ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-{{STRUCTURE_1zo8|  PDB=1zo8  |  SCENE=  }}
+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:16173767<ref>PMID:16173767</ref>
-===X-ray Structure of the haloalcohol dehalogenase HheC of Agrobacterium radiobacter AD1 in complex with (S)-para-nitrostyrene oxide, with a water molecule in the halide-binding site===
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-{{ABSTRACT_PUBMED_16173767}}
+==See Also==
+*[[Dehalogenase|Dehalogenase]]
-==About this Structure==
+== References ==
-[[1zo8]] is a 16 chain structure with 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=1ZO8 OCA].
+<references/>
+__TOC__
-==Reference==
+</StructureSection>
-<ref group="xtra">PMID:016173767</ref><references group="xtra"/>
 [[Category: Agrobacterium tumefaciens]]
 [[Category: Dijkstra, B W.]]