We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1qq7

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qq7.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1qq7.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1qq7| PDB=1qq7 | SCENE= }}
{{STRUCTURE_1qq7| PDB=1qq7 | SCENE= }}
-
'''STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS WITH CHLOROPROPIONIC ACID COVALENTLY BOUND'''
+
===STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS WITH CHLOROPROPIONIC ACID COVALENTLY BOUND===
-
==Overview==
+
<!--
-
The L-2-haloacid dehalogenase from the 1,2-dichloroethane-degrading bacterium Xanthobacter autotrophicus GJ10 catalyzes the hydrolytic dehalogenation of small L-2-haloalkanoates to their corresponding D-2-hydroxyalkanoates, with inversion of the configuration at the C(2) atom. The structure of the apoenzyme at pH 8 was refined at 1.5-A resolution. By lowering the pH, the catalytic activity of the enzyme was considerably reduced, allowing the crystal structure determination of the complexes with L-2-monochloropropionate and monochloroacetate at 1.7 and 2.1 A resolution, respectively. Both complexes showed unambiguous electron density extending from the nucleophile Asp(8) to the C(2) atom of the dechlorinated substrates corresponding to a covalent enzyme-ester reaction intermediate. The halide ion that is cleaved off is found in line with the Asp(8) Odelta1-C(2) bond in a halide-stabilizing cradle made up of Arg(39), Asn(115), and Phe(175). In both complexes, the Asp(8) Odelta2 carbonyl oxygen atom interacts with Thr(12), Ser(171), and Asn(173), which possibly constitute the oxyanion hole in the hydrolysis of the ester bond. The carboxyl moiety of the substrate is held in position by interactions with Ser(114), Lys(147), and main chain NH groups. The L-2-monochloropropionate CH(3) group is located in a small pocket formed by side chain atoms of Lys(147), Asn(173), Phe(175), and Asp(176). The size and position of the pocket explain the stereospecificity and the limited substrate specificity of the enzyme. These crystallographic results demonstrate that the reaction of the enzyme proceeds via the formation of a covalent enzyme-ester intermediate at the nucleophile Asp(8).
+
The line below this paragraph, {{ABSTRACT_PUBMED_10521454}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10521454 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10521454}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Rozeboom, H J.]]
[[Category: Rozeboom, H J.]]
[[Category: L-2-haloacid dehalogenase]]
[[Category: L-2-haloacid dehalogenase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:34:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:09:26 2008''

Revision as of 10:09, 28 July 2008

Image:1qq7.png

Template:STRUCTURE 1qq7

STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS WITH CHLOROPROPIONIC ACID COVALENTLY BOUND

Template:ABSTRACT PUBMED 10521454

About this Structure

1QQ7 is a Single protein structure of sequence from Xanthobacter autotrophicus. Full crystallographic information is available from OCA.

Reference

Crystal structures of intermediates in the dehalogenation of haloalkanoates by L-2-haloacid dehalogenase., Ridder IS, Rozeboom HJ, Kalk KH, Dijkstra BW, J Biol Chem. 1999 Oct 22;274(43):30672-8. PMID:10521454

Page seeded by OCA on Mon Jul 28 13:09:26 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qq7"
Personal tools