1d07: Difference between revisions

Revision as of 13:11, 21 February 2008

HYDROLYTIC HALOALKANE DEHALOGENASE LINB FROM SPHINGOMONAS PAUCIMOBILIS UT26 WITH 1,3-PROPANEDIOL, A PRODUCT OF DEBROMIDATION OF DIBROMPROPANE, AT 2.0A RESOLUTION

OverviewOverview

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.

About this StructureAbout this Structure

1D07 is a Single protein structure of sequence from Sphingomonas paucimobilis with and as ligands. Active as Haloalkane dehalogenase, with EC number 3.8.1.5 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

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OCA

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-[[Image:1d07.jpg|left|200px]]<br /><applet load="1d07" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1d07.jpg|left|200px]]<br /><applet load="1d07" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1d07, resolution 2.00&Aring;" />
 '''HYDROLYTIC HALOALKANE DEHALOGENASE LINB FROM SPHINGOMONAS PAUCIMOBILIS UT26 WITH 1,3-PROPANEDIOL, A PRODUCT OF DEBROMIDATION OF DIBROMPROPANE, AT 2.0A RESOLUTION'''<br />
 ==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 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.
 ==About this Structure==
-D07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sphingomonas_paucimobilis Sphingomonas paucimobilis] with BR and PDO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Haloalkane_dehalogenase Haloalkane dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.5 3.8.1.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D07 OCA].
+D07 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sphingomonas_paucimobilis Sphingomonas paucimobilis] with <scene name='pdbligand=BR:'>BR</scene> and <scene name='pdbligand=PDO:'>PDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Haloalkane_dehalogenase Haloalkane dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.5 3.8.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D07 OCA].
 ==Reference==
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 [[Category: Newman, J.]]
 [[Category: Smatanova, I.]]
-[[Category: Svensson, L.A.]]
+[[Category: Svensson, L A.]]
 [[Category: Takagi, M.]]
 [[Category: Vevodova, J.]]
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 [[Category: lindane]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:54:02 2007''
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