Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297
| Autor: | Kazutaka Murayama, Kota Kano, Yusaku Matsumoto, Daisuke Sugimori |
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| Rok vydání: | 2012 |
| Předmět: |
Models
Molecular Phospholipase A biology Molecular Structure Chemistry Stereochemistry Protein Conformation Molecular Sequence Data Active site Glycerophospholipids Phospholipases A1 Streptomyces Polyethylene Glycols Phospholipase A1 Species Specificity Structural Biology Catalytic Domain Hydrolase Catalytic triad biology.protein Molecular replacement Amino Acid Sequence Lipase Crystallization |
| Zdroj: | Journal of structural biology. 182(2) |
| ISSN: | 1095-8657 |
| Popis: | The metal-independent lipase from Streptomyces albidoflavus NA297 (SaPLA1) is a phospholipase A1 as it preferentially hydrolyzes the sn-1 acyl ester in glycerophospholipids, yielding a fatty acid and 2-acyl-lysophospholipid. The molecular mechanism underlying the substrate binding by SaPLA1 is currently unknown. In this study, the crystal structure of SaPLA1 was determined at 1.75 A resolutions by molecular replacement. A structural similarity search indicated the highest structural similarity to an esterase from Streptomyces scabies, followed by GDSL family enzymes. The SaPLA1 active site is composed of a Ser-His dyad (Ser11 and His218), whereby stabilization of the imidazole is provided by the main-chain carbonyl oxygen of Ser216, a common variation of the catalytic triad in many serine hydrolases, where this carbonyl maintains the orientation of the active site histidine residue. The hydrophobic pocket and cleft for lipid binding are adjacent to the active site, and are approximately 13–15 A deep and 14–16 A long. A partial polyethylene glycol structure was found in this hydrophobic pocket. |
| Databáze: | OpenAIRE |
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