1G4I

Crystal structure of the bovine pancreatic phospholipase A2 at 0.97A

Summary for 1G4I

• Entry DOI: 10.2210/pdb1g4i/pdb
• Related: 1BP2 1UNE
• Descriptor: PHOSPHOLIPASE A2, CALCIUM ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: lipid degradation, hydrolase
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P00593
• Total number of polymer chains: 1
• Total formula weight: 14476.91

Authors

Steiner, R.A.,Rozeboom, H.J.,de Vries, A.,Kalk, K.H.,Murshudov, G.N.,Wilson, K.S.,Dijkstra, B.W. (deposition date: 2000-10-27, release date: 2001-04-04, Last modification date: 2024-11-13)

Primary citation

Steiner, R.A.,Rozeboom, H.J.,de Vries, A.,Kalk, K.H.,Murshudov, G.N.,Wilson, K.S.,Dijkstra, B.W.
X-ray structure of bovine pancreatic phospholipase A2 at atomic resolution.
Acta Crystallogr.,Sect.D, 57:516-526, 2001

PubMed Abstract: Using synchrotron radiation and a CCD camera, X-ray data have been collected from wild-type bovine pancreatic phospholipase A(2) at 100 K to 0.97 A resolution allowing full anisotropic refinement. The final model has a conventional R factor of 9.44% for all reflections, with a mean standard uncertainty for the positional parameters of 0.031 A as calculated from inversion of the full positional least-squares matrix. At 0.97 A resolution, bovine pancreatic phospholipase A(2) reveals for the first time that its rigid scaffolding does not preclude flexibility, which probably plays an important role in the catalytic process. Functionally important regions (the interfacial binding site and calcium-binding loop) are located at the molecular surface, where conformational variability is more pronounced. A cluster of 2-methyl-2,4-pentanediol molecules is present at the entrance of the hydrophobic channel that leads to the catalytic site and mimics the fatty-acid chains of a substrate analogue. Bovine pancreatic phospholipase A(2) at atomic resolution is compared with previous crystallographic structures and with models derived from nuclear magnetic resonance studies. Given the high structural similarity among extracellular phospholipases A(2) observed so far at lower resolution, the results arising from this structural analysis are expected to be of general validity for this class of enzymes.

PubMed: 11264580
DOI: 10.1107/S0907444901002530

Experimental method

X-RAY DIFFRACTION (0.97 Å)