2czq

A novel cutinase-like protein from Cryptococcus sp.

spinqualitylabelsall models 2czq, resolution 1.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2czq is a 2 chain structure with sequence from Cryptococcus sp. S-2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.05Å Ligands: CIT, EDO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q874E9_9TREE 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 The structural and enzymatic characteristics of a cutinase-like enzyme (CLE) from Cryptococcus sp. strain S-2, which exhibits remote homology to a lipolytic enzyme and a cutinase from the fungus Fusarium solani (FS cutinase), were compared to investigate the unique substrate specificity of CLE. The crystal structure of CLE was solved to a 1.05 A resolution. Moreover, hydrolysis assays demonstrated the broad specificity of CLE for short and long-chain substrates, as well as the preferred specificity of FS cutinase for short-chain substrates. In addition, site-directed mutagenesis was performed to increase the hydrolysis activity on long-chain substrates, indicating that the hydrophobic aromatic residues are important for the specificity to the long-chain substrate. These results indicate that hydrophobic residues, especially the aromatic ones exposed to solvent, are important for retaining lipase activity. Crystal structure and enhanced activity of a cutinase-like enzyme from Cryptococcus sp. strain S-2.,Kodama Y, Masaki K, Kondo H, Suzuki M, Tsuda S, Nagura T, Shimba N, Suzuki E, Iefuji H Proteins. 2009 Nov 15;77(3):710-7. PMID:19544571 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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