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1iz8

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{{STRUCTURE_1iz8| PDB=1iz8 | SCENE= }}
{{STRUCTURE_1iz8| PDB=1iz8 | SCENE= }}
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'''Re-refinement of the structure of hydrolytic haloalkane dehalogenase linb from sphingomonas paucimobilis UT26 with 1,3-propanediol, a product of debromidation of dibrompropane, at 2.0A resolution'''
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===Re-refinement of the structure of hydrolytic haloalkane dehalogenase linb from sphingomonas paucimobilis UT26 with 1,3-propanediol, a product of debromidation of dibrompropane, at 2.0A resolution===
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==Overview==
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The haloalkane dehalogenases are detoxifying enzymes that convert a broad range of halogenated substrates to the corresponding alcohols. Complete crystal structures of haloalkane dehalogenase from Sphingomonas paucimobilis UT26 (LinB), and complexes of LinB with 1,2-propanediol/1-bromopropane-2-ol and 2-bromo-2-propene-1-ol, products of debromination of 1,2-dibromopropane and 2,3-dibromopropene, respectively, were determined from 1.8 A resolution X-ray diffraction data. Published structures of native LinB and its complex with 1,3-propanediol [Marek et al. (2000) Biochemistry 39, 14082-14086] were reexamined. The full and partial debromination of 1,2-dibromopropane and 2,3-dibromopropene, respectively, conformed to the observed general trend that the sp(3)-hybridized carbon is the predominant electrophilic site for the S(N)2 bimolecular nucleophilic substitution in dehalogenation reaction. The 2-bromo-2-propene-1-ol product of 2,3-dibromopropene dehalogenation in crystal was positively identified by the gas chromatography-mass spectroscopy (GC-MS) technique. The 1,2-propanediol and 1-bromopropane-2-ol products of 1,2-dibromopropane dehalogenation in crystal were also supported by the GC-MS identification. Comparison of native LinB with its complexes showed high flexibility of residues 136-157, in particular, Asp146 and Glu147, from the cap domain helices alpha(4) and alpha(5)('). Those residues were shifted mainly in direction toward the ligand molecules in the complex structures. It seems the cap domain moves nearer to the core squeezing substrate into the active center closer to the catalytic triad. This also leads to slight contraction of the whole complex structures. The flexibility detected by crystallographic analysis is in remarkable agreement with flexibility observed by molecular dynamic simulations.
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{{ABSTRACT_PUBMED_12939138}}
==About this Structure==
==About this Structure==
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[[Category: Dehalogenase]]
[[Category: Dehalogenase]]
[[Category: Lindane]]
[[Category: Lindane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:26:52 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 14:15:32 2008''

Revision as of 11:15, 1 July 2008

Image:1iz8.png

Template:STRUCTURE 1iz8

Re-refinement of the structure of hydrolytic haloalkane dehalogenase linb from sphingomonas paucimobilis UT26 with 1,3-propanediol, a product of debromidation of dibrompropane, at 2.0A resolution

Template:ABSTRACT PUBMED 12939138

About this Structure

1IZ8 is a Single protein structure of sequence from Sphingomonas paucimobilis. Full crystallographic information is available from OCA.

Reference

Haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26: X-ray crystallographic studies of dehalogenation of brominated substrates., Streltsov VA, Prokop Z, Damborsky J, Nagata Y, Oakley A, Wilce MC, Biochemistry. 2003 Sep 2;42(34):10104-12. PMID:12939138

Page seeded by OCA on Tue Jul 1 14:15:32 2008

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