1ziy: Difference between revisions

Revision as of 08:23, 28 July 2008

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File:1ziy.png

Template:STRUCTURE 1ziy

Crystal Structure Analysis of the dienelactone hydrolase mutant (C123S) bound with the PMS moiety of the protease inhibitor, Phenylmethylsulfonyl fluoride (PMSF)- 1.9 ACrystal Structure Analysis of the dienelactone hydrolase mutant (C123S) bound with the PMS moiety of the protease inhibitor, Phenylmethylsulfonyl fluoride (PMSF)- 1.9 A

Template:ABSTRACT PUBMED 15983415

About this StructureAbout this Structure

1ZIY is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.

ReferenceReference

Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase., Kim HK, Liu JW, Carr PD, Ollis DL, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):920-31. Epub 2005, Jun 24. PMID:15983415

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OCA

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-[[Image:1ziy.gif|left|200px]]
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 {{STRUCTURE_1ziy|  PDB=1ziy  |  SCENE=  }}
-'''Crystal Structure Analysis of the dienelactone hydrolase mutant (C123S) bound with the PMS moiety of the protease inhibitor, Phenylmethylsulfonyl fluoride (PMSF)- 1.9 A'''
+===Crystal Structure Analysis of the dienelactone hydrolase mutant (C123S) bound with the PMS moiety of the protease inhibitor, Phenylmethylsulfonyl fluoride (PMSF)- 1.9 A===
-==Overview==
+<!--
-The enzyme dienelactone hydrolase (DLH) has undergone directed evolution to produce a series of mutant proteins that have enhanced activity towards the non-physiological substrates alpha-naphthyl acetate and p-nitrophenyl acetate. In terms of steady-state kinetics, the mutations caused a drop in the K(m) for the hydrolysis reaction with these two substrates. For the best mutant, there was a 5.6-fold increase in k(cat)/K(m) for the hydrolysis of alpha-naphthyl acetate and a 3.6-fold increase was observed for p-nitrophenyl acetate. For alpha-naphthyl acetate the pre-steady-state kinetics revealed that the rate constant for the formation of the covalent intermediate had increased. The mutations responsible for the rate enhancements map to the active site. The structures of the starting and mutated proteins revealed small changes in the protein owing to the mutations, while the structures of the same proteins with an inhibitor co-crystallized in the active site indicated that the mutations caused significant changes in the way the mutated proteins recognized the substrates. Within the active site of the mutant proteins, the inhibitor was rotated by about 180 degrees with respect to the orientation found in the starting enzyme. This rotation of the inhibitor caused the displacement of a large section of a loop on one side of the active site. Residues that could stabilize the transition state for the reaction were identified.
+The line below this paragraph, {{ABSTRACT_PUBMED_15983415}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15983415 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15983415}}
 ==About this Structure==
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 [[Category: Pmsf]]
 [[Category: Serine esterase]]
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