1VKQ

A re-determination of the structure of the triple mutant (K53,56,120M) of phospholipase A2 at 1.6A resolution using sulphur-SAS at 1.54A wavelength

Summary for 1VKQ

• Entry DOI: 10.2210/pdb1vkq/pdb
• Descriptor: Phospholipase A2, CALCIUM ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: alpha helix, beta sheet, triple mutant, calcium ion, hydrolase
• Biological source: Bos taurus (cattle)
• Cellular location: Secreted: P00593
• Total number of polymer chains: 1
• Total formula weight: 14246.60

Authors

Sekar, K.,Velmurugan, D.,Rajakannan, V.,Yamane, T.,Dauter, M.,Dauter, Z. (deposition date: 2004-06-12, release date: 2004-08-31, Last modification date: 2023-12-27)

Primary citation

Sekar, K.,Rajakannan, V.,Velmurugan, D.,Yamane, T.,Thirumurugan, R.,Dauter, M.,Dauter, Z.
A redetermination of the structure of the triple mutant (K53,56,120M) of phospholipase A2 at 1.6 A resolution using sulfur-SAS at 1.54 A wavelength.
Acta Crystallogr.,Sect.D, 60:1586-1590, 2004

PubMed Abstract: The crystal structure of the triple mutant K53,56,120M of bovine pancreatic phospholipase A(2) has been redetermined using sulfur single-wavelength anomalous scattering. The synchrotron data were collected at lambda = 1.54 A and the crystal diffracted to 1.6 A resolution. The program SOLVE was used to locate the heavy atoms and to estimate the initial phases and the resulting map was then subjected to RESOLVE. The output of 455 non-H atoms, including 12 S atoms, one calcium ion and one chloride ion, were then subjected to ARP/wARP followed by REFMAC. With the improved phases, the automatic model building successfully built more than 85% of the 123 residues, excluding the N- and C-terminal residues. The final crystallographic R factor is 17.7% (R(free) = 21.7%). The refined model consists of 954 non-H protein atoms, 165 water O atoms, three 2-methyl-2,4-pentanediol (MPD) molecules, one calcium ion and one chloride ion. The present work is yet another example that shows the utility of single-wavelength anomalous scattering data for solving a protein structure.

PubMed: 15333929
DOI: 10.1107/S090744490401697X

Experimental method

X-RAY DIFFRACTION (1.6 Å)