1din: Difference between revisions
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[[Image:1din.jpg|left|200px]] | [[Image:1din.jpg|left|200px]] | ||
'''DIENELACTONE HYDROLASE AT 2.8 ANGSTROMS''' | {{Structure | ||
|PDB= 1din |SIZE=350|CAPTION= <scene name='initialview01'>1din</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Carboxymethylenebutenolidase Carboxymethylenebutenolidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.45 3.1.1.45] | |||
|GENE= CLC D ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=306 Pseudomonas sp.]) | |||
}} | |||
'''DIENELACTONE HYDROLASE AT 2.8 ANGSTROMS''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1DIN is a [ | 1DIN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_sp. Pseudomonas sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DIN OCA]. | ||
==Reference== | ==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:[http:// | Refined structure of dienelactone hydrolase at 1.8 A., Pathak D, Ollis D, J Mol Biol. 1990 Jul 20;214(2):497-525. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2380986 2380986] | ||
[[Category: Carboxymethylenebutenolidase]] | [[Category: Carboxymethylenebutenolidase]] | ||
[[Category: Pseudomonas sp.]] | [[Category: Pseudomonas sp.]] | ||
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[[Category: serine esterase]] | [[Category: serine esterase]] | ||
''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 10:39:07 2008'' | ||
Revision as of 11:39, 20 March 2008
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| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | CLC D (Pseudomonas sp.) | ||||||
| Activity: | Carboxymethylenebutenolidase, with EC number 3.1.1.45 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DIENELACTONE HYDROLASE AT 2.8 ANGSTROMS
OverviewOverview
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.
About this StructureAbout this Structure
1DIN is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.
ReferenceReference
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
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