Crystallization and preliminary X-ray studies of the protease domain of the heat-shock protein HtrA from Thermotoga maritima.
HtrA (high-temperature requirement A) is a widely distributed heat-shock protein which has both molecular-chaperone and proteolytic activities. It is composed of two PDZ domains essential for oligomerization and a protease domain. To understand the molecular basis of the dual function of HtrA, the protease domain of T. maritima HtrA has been crystallized. X-ray diffraction data have been collected to 2.7 A resolution using a synchrotron-radiation source. Crystals belong to the cubic space group P2(1)3, with unit-cell parameters a = b = c = 120.55 (8) A. The asymmetric unit contains two protease domains, with a corresponding V(M) of 2.80 A(3) Da(-1) and a solvent content of 56.1%.
Kim
Dong Young
DY
Department of Molecular Cell Biology, Center for Molecular Medicine, SBRI, Sungkyunkwan University School of Medicine, Suwon 440-746, South Korea.
Kim
Kyeong Kyu
KK
D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D006360:Heat-Shock Proteins / Q000737:chemistry*; D033903:Periplasmic Proteins; D011487:Protein Conformation; D012697:Serine Endopeptidases / Q000737:chemistry*; D020124:Thermotoga maritima / Q000737:chemistry*
D017931:DNA Primers; D006360:Heat-Shock Proteins; D033903:Periplasmic Proteins; C061682:DegP protease; D012697:Serine Endopeptidases