1zmt: Difference between revisions

Revision as of 20:33, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1zmt.png

Template:STRUCTURE 1zmt

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

Template:ABSTRACT PUBMED 16173767

About this StructureAbout this Structure

1ZMT is a Single protein structure of sequence from Agrobacterium tumefaciens. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Sun Jul 27 20:33:15 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1zmt.gif|left|200px]]
+{{Seed}}
+[[Image:1zmt.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1zmt|  PDB=1zmt  |  SCENE=  }}
-'''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'''
+===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===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_16173767}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16173767 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16173767}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Haloalcohol dehalogenase]]
 [[Category: Halohydrin dehalogenase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:49:17 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 20:33:15 2008''