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1bn6
From Proteopedia
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(New page: 200px<br /> <applet load="1bn6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bn6, resolution 1.5Å" /> '''HALOALKANE DEHALOGEN...)
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Revision as of 19:59, 29 October 2007
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HALOALKANE DEHALOGENASE FROM A RHODOCOCCUS SPECIES
Overview
The hydrolytic haloalkane dehalogenases are promising bioremediation and, biocatalytic agents. Two general classes of dehalogenases have been, reported from Xanthobacter and Rhodococcus. While these enzymes share 30%, amino acid sequence identity, they have significantly different substrate, specificities and halide-binding properties. We report the 1.5 A, resolution crystal structure of the Rhodococcus dehalogenase at pH 5.5, pH, 7.0, and pH 5.5 in the presence of NaI. The Rhodococcus and Xanthobacter, enzymes have significant structural homology in the alpha/beta hydrolase, core, but differ considerably in the cap domain. Consistent with its broad, specificity for primary, secondary, and cyclic haloalkanes, the, Rhodococcus enzyme has a substantially larger active site cavity., ... [(full description)]
About this Structure
1BN6 is a [Single protein] structure of sequence from [Rhodococcus sp.]. Active as [[1]], with EC number [3.8.1.5]. Full crystallographic information is available from [OCA].
Reference
Haloalkane dehalogenases: structure of a Rhodococcus enzyme., Newman J, Peat TS, Richard R, Kan L, Swanson PE, Affholter JA, Holmes IH, Schindler JF, Unkefer CJ, Terwilliger TC, Biochemistry. 1999 Dec 7;38(49):16105-14. PMID:10587433
Page seeded by OCA on Mon Oct 29 22:04:27 2007
