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| | {{STRUCTURE_1din| PDB=1din | SCENE= }} | | {{STRUCTURE_1din| PDB=1din | SCENE= }} |
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| - | '''DIENELACTONE HYDROLASE AT 2.8 ANGSTROMS'''
| + | ===DIENELACTONE HYDROLASE AT 2.8 ANGSTROMS=== |
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| - | ==Overview==
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| - | The structure of dienelactone hydrolase (DLH) from Pseudomonus sp. B13, after stereochemically restrained least-squares refinement at 1.8 A resolution, is described. The final molecular model of DLH has a conventional R value of 0.150 and includes all but the carboxyl-terminal three residues that are crystallographically disordered. The positions of 279 water molecules are included in the final model. The root-mean-square deviation from ideal bond distances for the model is 0.014 A and the error in atomic co-ordinates is estimated to be 0.15 A. DLH is a monomeric enzyme containing 236 amino acid residues and is a member of the beta-ketoadipate pathway found in bacteria and fungi. DLH is an alpha/beta protein containing seven helices and eight strands of beta-pleated sheet. A single 4-turn 3(10)-helix is seen. The active-site Cys123 residues at the N-terminal end of an alpha-helix that is peculiar in its consisting entirely of hydrophobic residues (except for a C-terminal lysine). The beta-sheet is composed of parallel strands except for strand 2, which gives rise to a short antiparallel region at the N-terminal end of the central beta-sheet. The active-site cysteine residue is part of a triad of residues consisting of Cys123, His202 and Asp171, and is reminiscent of the serine/cysteine proteases. As in papain and actinidin, the active thiol is partially oxidized during X-ray data collection. The positions of both the reduced and the oxidized sulphur are described. The active site geometry suggests that a change in the conformation of the native thiol occurs upon diffusion of substrate into the active site cleft of DLH. This enables nucleophilic attack by the gamma-sulphur to occur on the cyclic ester substrate through a ring-opening reaction. | + | The line below this paragraph, {{ABSTRACT_PUBMED_2380986}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 2380986 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_2380986}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hydrolytic enzyme]] | | [[Category: Hydrolytic enzyme]] |
| | [[Category: Serine esterase]] | | [[Category: Serine esterase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:53:18 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:07:16 2008'' |
Revision as of 20:07, 30 June 2008
Template:STRUCTURE 1din
DIENELACTONE HYDROLASE AT 2.8 ANGSTROMS
Template:ABSTRACT PUBMED 2380986
About this Structure
1DIN is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.
Reference
Refined structure of dienelactone hydrolase at 1.8 A., Pathak D, Ollis D, J Mol Biol. 1990 Jul 20;214(2):497-525. PMID:2380986
Page seeded by OCA on Mon Jun 30 23:07:16 2008
