4hyq

Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297

spinqualitylabelsall models 4hyq, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4hyq is a 1 chain structure with sequence from Streptomyces albidoflavus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: 1PE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function K0J3J2_9ACTN Publication Abstract from PubMed 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 1.75A 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 13-15A deep and 14-16A long. A partial polyethylene glycol structure was found in this hydrophobic pocket. Crystal structure of phospholipase A1 from Streptomyces albidoflavus NA297.,Murayama K, Kano K, Matsumoto Y, Sugimori D J Struct Biol. 2013 May;182(2):192-6. doi: 10.1016/j.jsb.2013.02.003. Epub 2013, Feb 13. PMID:23416196 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phospholipase A1

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