1cus | pdb_00001cus

FUSARIUM SOLANI CUTINASE IS A LIPOLYTIC ENZYME WITH A CATALYTIC SERINE ACCESSIBLE TO SOLVENT

spinqualitylabelsall models 1cus, resolution 1.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1cus is a 1 chain structure with sequence from Fusso. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [CUTI1_FUSSO] Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Allows pathogenic fungi to penetrate through the cuticular barrier into the host plant during the initial stage of the fungal infection. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Lipases belong to a class of esterases whose activity on triglycerides is greatly enhanced at lipid-water interfaces. This phenomenon, called interfacial activation, has a structural explanation: a hydrophobic lid, which at rest covers the catalytic site, is displaced on substrate or inhibitor binding and probably interacts with the lipid matrix. Fusarium solani pisi cutinase belongs to a group of homologous enzymes of relative molecular mass 22-25K (ref. 7) capable of degrading cutin, the insoluble lipid-polyester matrix covering the surface of plants, and hydrolysing triglycerides. Cutinases differ from classical lipases in that they do not exhibit interfacial activation; they are active on soluble as well as on emulsified triglycerides. Cutinases therefore establish a bridge between esterases and lipases. We report here the three-dimensional structure of a recombinant cutinase from F. solani pisi, expressed in Escherichia coli. Cutinase is an alpha-beta protein; the active site is composed of the triad Ser 120, His 188 and Asp 175. Unlike other lipases, the catalytic serine is not buried under surface loops, but is accessible to solvent. This could explain why cutinase does not display interfacial activation. Fusarium solani cutinase is a lipolytic enzyme with a catalytic serine accessible to solvent.,Martinez C, De Geus P, Lauwereys M, Matthyssens G, Cambillau C Nature. 1992 Apr 16;356(6370):615-8. PMID:1560844 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Cutinase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA