2CZQ
A novel cutinase-like protein from Cryptococcus sp.
Summary for 2CZQ
| Entry DOI | 10.2210/pdb2czq/pdb |
| Descriptor | cutinase-like protein, CITRIC ACID, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | alpha/beta hydrolase fold, hydrolase |
| Biological source | Cryptococcus sp. |
| Total number of polymer chains | 2 |
| Total formula weight | 42368.50 |
| Authors | Masaki, K.,Kamini, N.R.,Ikeda, H.,Iefuji, H.,Kondo, H.,Suzuki, M.,Tsuda, S. (deposition date: 2005-07-14, release date: 2006-07-14, Last modification date: 2024-11-20) |
| Primary citation | Kodama, Y.,Masaki, K.,Kondo, H.,Suzuki, M.,Tsuda, S.,Nagura, T.,Shimba, N.,Suzuki, E.,Iefuji, H. Crystal structure and enhanced activity of a cutinase-like enzyme from Cryptococcus sp. strain S-2 Proteins, 77:710-717, 2009 Cited by PubMed Abstract: 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. PubMed: 19544571DOI: 10.1002/prot.22484 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.05 Å) |
Structure validation
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