1cuc: Difference between revisions

Revision as of 13:09, 21 February 2008

CUTINASE, N172K, R196D MUTANT, ORTHORHOMBIC CRYSTAL FORM

OverviewOverview

In characterizing mutants and covalently inhibited complexes of Fusarium solani cutinase, which is a 197-residue lipolytic enzyme, 34 variant structures, crystallizing in 8 different crystal forms, have been determined, mostly at high resolution. Taking advantage of this considerable body of information, a structural comparative analysis was carried out to investigate the dynamics of cutinase. Surface loops were identified as the major flexible protein regions, particularly those forming the active-site groove, whereas the elements constituting the protein scaffold were found to retain the same conformation in all the cutinase variants studied. Flexibility turned out to be correlated with thermal motion. With a given crystal packing environment, a high flexibility turned out to be correlated with a low involvement in crystal packing contacts. The high degree of crystal polymorphism, which allowed different conformations with similar energy to be detected, made it possible to identify motions which would have remained unidentified if only a single crystal form had been available. Fairly good agreement was found to exist between the data obtained from the structural comparison and those from a molecular dynamics (MD) simulation carried out on the native enzyme. The crystallographic approach used in this study turned out to be a suitable tool for investigating cutinase dynamics. Because of the availability of a set of closely related proteins in different crystal environments, the intrinsic drawback of a crystallographic approach was bypassed. By combining several static pictures, the dynamics of the protein could be monitored much more realistically than what can be achieved on the basis of static pictures alone.

About this StructureAbout this Structure

1CUC is a Single protein structure of sequence from Fusarium solani subsp. pisi. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants., Longhi S, Nicolas A, Creveld L, Egmond M, Verrips CT, de Vlieg J, Martinez C, Cambillau C, Proteins. 1996 Dec;26(4):442-58. PMID:8990497

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 ==Overview==
-In characterizing mutants and covalently inhibited complexes of Fusarium, solani cutinase, which is a 197-residue lipolytic enzyme, 34 variant, structures, crystallizing in 8 different crystal forms, have been, determined, mostly at high resolution. Taking advantage of this, considerable body of information, a structural comparative analysis was, carried out to investigate the dynamics of cutinase. Surface loops were, identified as the major flexible protein regions, particularly those, forming the active-site groove, whereas the elements constituting the, protein scaffold were found to retain the same conformation in all the, cutinase variants studied. Flexibility turned out to be correlated with, thermal motion. With a given crystal packing environment, a high, flexibility turned out to be correlated with a low involvement in crystal, packing contacts. The high degree of crystal polymorphism, which allowed, different conformations with similar energy to be detected, made it, possible to identify motions which would have remained unidentified if, only a single crystal form had been available. Fairly good agreement was, found to exist between the data obtained from the structural comparison, and those from a molecular dynamics (MD) simulation carried out on the, native enzyme. The crystallographic approach used in this study turned out, to be a suitable tool for investigating cutinase dynamics. Because of the, availability of a set of closely related proteins in different crystal, environments, the intrinsic drawback of a crystallographic approach was, bypassed. By combining several static pictures, the dynamics of the, protein could be monitored much more realistically than what can be, achieved on the basis of static pictures alone.
+In characterizing mutants and covalently inhibited complexes of Fusarium solani cutinase, which is a 197-residue lipolytic enzyme, 34 variant structures, crystallizing in 8 different crystal forms, have been determined, mostly at high resolution. Taking advantage of this considerable body of information, a structural comparative analysis was carried out to investigate the dynamics of cutinase. Surface loops were identified as the major flexible protein regions, particularly those forming the active-site groove, whereas the elements constituting the protein scaffold were found to retain the same conformation in all the cutinase variants studied. Flexibility turned out to be correlated with thermal motion. With a given crystal packing environment, a high flexibility turned out to be correlated with a low involvement in crystal packing contacts. The high degree of crystal polymorphism, which allowed different conformations with similar energy to be detected, made it possible to identify motions which would have remained unidentified if only a single crystal form had been available. Fairly good agreement was found to exist between the data obtained from the structural comparison and those from a molecular dynamics (MD) simulation carried out on the native enzyme. The crystallographic approach used in this study turned out to be a suitable tool for investigating cutinase dynamics. Because of the availability of a set of closely related proteins in different crystal environments, the intrinsic drawback of a crystallographic approach was bypassed. By combining several static pictures, the dynamics of the protein could be monitored much more realistically than what can be achieved on the basis of static pictures alone.
 ==About this Structure==
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 [[Category: serine esterase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:34:56 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:45 2008''