Crystal structure of a triacylglycerol lipase from Penicillum expansum at 1.3 A determined by sulfur SAD

Fujian Institute of Research on the Structure of Matter, Chinese Academy of Sciences, Fuzhou, China.
Proteins Structure Function and Bioinformatics (Impact Factor: 2.63). 05/2010; 78(6):1601-5. DOI: 10.1002/prot.22676
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Available from: Mingdong Huang, Sep 21, 2014
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    • "These three lipases have identical sequences. The crystal structure has been solved for one of the two P. expansum lipases discussed above (AAK07480; Bian et al. 2010) and this enabled determining the position of the residues, Ser (159)–Asp (215)–His (268), which constitute the catalytic triad of LipPE (Fig. 3). A multiple sequence alignment of LipPE and other four lipases with the highest identity demonstrated that the active-site sequence (GHSLG) was identical at the amino acid level (supplementary Fig. 1). "
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