Atomic resolution structure of the double mutant (K53,56M) of bovine pancreatic phospholipase A2.
The structure of the double mutant K53,56M has previously been refined at 1.9 A resolution using room-temperature data. The present paper reports the crystal structure of the same mutant K53,56M refined against 1.1 A data collected using synchrotron radiation. A total of 116 main-chain atoms from 29 residues and 44 side chains are modelled in alternate conformations. Most of the interfacial binding residues are found to be disordered and alternate conformations could be recognized. The second calcium ion-binding site residue Glu92 adopts two alternate conformations. The minor and major conformations of Glu92 correspond to the second calcium ion bound and unbound states.
Sekar
K
K
Bioinformatics Centre, Indian Institute of Science, Bangalore 560 012, India. sekar@physics.iisc.ernet.in
Yogavel
M
M
Gayathri
D
D
Velmurugan
D
D
Krishna
R
R
Poi
M-J
MJ
Dauter
Z
Z
Dauter
M
M
Tsai
M-D
MD
D000818:Animals; D001665:Binding Sites / Q000235:genetics; D002118:Calcium / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D002417:Cattle; D018360:Crystallography, X-Ray; D008239:Lysine / Q000235:genetics; D008715:Methionine / Q000235:genetics; D010741:Phospholipases A / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D054467:Phospholipases A2; D017354:Point Mutation; D011487:Protein Conformation
D002135:Calcium-Binding Proteins; D008715:Methionine; D010741:Phospholipases A; D054467:Phospholipases A2; D008239:Lysine; D002118:Calcium