Open AccessAtomic resolution structure of the double mutant (K53,56M) of bovine pancreatic phospholipase A 2
Author(s) -
Sekar K.,
Yogavel M.,
Gayathri D.,
Velmurugan D.,
Krishna R.,
Poi M.J.,
Dauter Z.,
Dauter M.,
Tsai M.D.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105040984
Subject(s) - crystallography , mutant , crystal structure , chemistry , ion , synchrotron radiation , residue (chemistry) , calcium , side chain , biochemistry , physics , organic chemistry , quantum mechanics , gene , polymer
The structure of the double mutant K53,56M has previously been refined at 1.9 Å resolution using room‐temperature data. The present paper reports the crystal structure of the same mutant K53,56M refined against 1.1 Å 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.