1cv2
From Proteopedia
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| - | [[Image:1cv2.gif|left|200px]] | + | [[Image:1cv2.gif|left|200px]] |
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| - | '''HYDROLYTIC HALOALKANE DEHALOGENASE LINB FROM SPHINGOMONAS PAUCIMOBILIS UT26 AT 1.6 A RESOLUTION''' | + | {{Structure |
| + | |PDB= 1cv2 |SIZE=350|CAPTION= <scene name='initialview01'>1cv2</scene>, resolution 1.58Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HYDROLYTIC HALOALKANE DEHALOGENASE LINB FROM SPHINGOMONAS PAUCIMOBILIS UT26 AT 1.6 A RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CV2 is a [ | + | 1CV2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sphingomonas_paucimobilis Sphingomonas paucimobilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CV2 OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11087355 11087355] |
[[Category: Haloalkane dehalogenase]] | [[Category: Haloalkane dehalogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lindane]] | [[Category: lindane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:29:14 2008'' |
Revision as of 08:29, 20 March 2008
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| , resolution 1.58Å | |||||||
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| Activity: | Haloalkane dehalogenase, with EC number 3.8.1.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HYDROLYTIC HALOALKANE DEHALOGENASE LINB FROM SPHINGOMONAS PAUCIMOBILIS UT26 AT 1.6 A 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.
About this Structure
1CV2 is a Single protein structure of sequence from Sphingomonas paucimobilis. Full crystallographic information is available from OCA.
Reference
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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