1cuc: Difference between revisions
No edit summary |
No edit summary |
||
| Line 21: | Line 21: | ||
[[Category: serine esterase]] | [[Category: serine esterase]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:59:51 2007'' | ||
Revision as of 15:55, 30 October 2007
|
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 ... [(full description)]
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]. Structure known Active Site: CAT. 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
Page seeded by OCA on Tue Oct 30 14:59:51 2007