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| {{STRUCTURE_3bjx| PDB=3bjx | SCENE= }} | | {{STRUCTURE_3bjx| PDB=3bjx | SCENE= }} |
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| '''Structure of a Group I haloacid dehalogenase from Pseudomonas putida strain PP3'''
| | ===Structure of a Group I haloacid dehalogenase from Pseudomonas putida strain PP3=== |
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| ==Overview==
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| Haloacid dehalogenases catalyse the removal of halides from organic haloacids and are of interest for bioremediation and for their potential use in the synthesis of industrial chemicals. We present the crystal structure of the homodimer DehI from Pseudomonas putida strain PP3, the first structure of a group I alpha-haloacid dehalogenase that can process both l- and d-substrates. The structure shows that the DehI monomer consists of two domains of approximately 130 amino acids that have approximately 16% sequence identity yet adopt virtually identical and unique folds that form a pseudo-dimer. Analysis of the active site reveals the likely binding mode of both l- and d-substrates with respect to key catalytic residues. Asp189 is predicted to activate a water molecule for nucleophilic attack of the substrate chiral centre resulting in an inversion of configuration of either l- or d-substrates in contrast to d-only enzymes. These details will assist with future bioengineering of dehalogenases.
| | The line below this paragraph, {{ABSTRACT_PUBMED_18353360}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 18353360 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_18353360}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| [[Category: Plasmid]] | | [[Category: Plasmid]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:33:06 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:36:56 2008'' |
