1d07: Difference between revisions

Revision as of 21:54, 30 June 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:1d07.png

Template:STRUCTURE 1d07

Hydrolytic haloalkane dehalogenase linb from sphingomonas paucimobilis UT26 with 1,3-propanediol, a product of debromidation of dibrompropane, at 2.0A resolutionHydrolytic haloalkane dehalogenase linb from sphingomonas paucimobilis UT26 with 1,3-propanediol, a product of debromidation of dibrompropane, at 2.0A resolution

Template:ABSTRACT PUBMED 11087355

About this StructureAbout this Structure

1D07 is a Single protein structure of sequence from Sphingomonas paucimobilis. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the haloalkane dehalogenase from Sphingomonas paucimobilis UT26., Marek J, Vevodova J, Smatanova IK, Nagata Y, Svensson LA, Newman J, Takagi M, Damborsky J, Biochemistry. 2000 Nov 21;39(46):14082-6. PMID:11087355

Page seeded by OCA on Mon Jun 30 21:54:58 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1d07.jpg|left|200px]]
+{{Seed}}
+[[Image:1d07.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1d07|  PDB=1d07  |  SCENE=  }}
-'''Hydrolytic haloalkane dehalogenase linb from sphingomonas paucimobilis UT26 with 1,3-propanediol, a product of debromidation of dibrompropane, at 2.0A resolution'''
+===Hydrolytic haloalkane dehalogenase linb from sphingomonas paucimobilis UT26 with 1,3-propanediol, a product of debromidation of dibrompropane, at 2.0A resolution===
-==Overview==
+<!--
-The haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB) is the enzyme involved in the degradation of the important environmental pollutant gamma-hexachlorocyclohexane. The enzyme hydrolyzes a broad range of halogenated cyclic and aliphatic compounds. Here, we present the 1.58 A crystal structure of LinB and the 2.0 A structure of LinB with 1,3-propanediol, a product of debromination of 1,3-dibromopropane, in the active site of the enzyme. The enzyme belongs to the alpha/beta hydrolase family and contains a catalytic triad (Asp108, His272, and Glu132) in the lipase-like topological arrangement previously proposed from mutagenesis experiments. The LinB structure was compared with the structures of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10 and from Rhodococcus sp. and the structural features involved in the adaptation toward xenobiotic substrates were identified. The arrangement and composition of the alpha-helices in the cap domain results in the differences in the size and shape of the active-site cavity and the entrance tunnel. This is the major determinant of the substrate specificity of this haloalkane dehalogenase.
+The line below this paragraph, {{ABSTRACT_PUBMED_11087355}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11087355 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11087355}}
 ==About this Structure==
@@ Line 35: / Line 39: @@
 [[Category: Dehalogenase]]
 [[Category: Lindane]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun  5 09:52:58 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 21:54:58 2008''