Cloning, purification, crystallization and preliminary crystallographic analysis of a penicillin-binding protein homologue from Pyrococcus abyssi.
The genome of the hyperthermophilic archaeon Pyrococcus abyssi contains a gene (pab0087) encoding a penicillin-binding protein (PBP) homologue. This sequence consists of 447 residues and shows significant sequence similarity to low-molecular-weight PBPs and class C beta-lactamases. The Pab0087 protein was overexpressed, purified and crystallized. Diffraction data from two different crystal forms were collected to 2.7 and 2.0 A resolution. Both crystals belong to space group C2, with unit-cell parameters a = 160.59, b = 135.74, c = 113.02 A, beta = 117.36 degrees and a = 166.97, b = 131.25, c = 189.39 A, beta = 113.81 degrees , respectively. The asymmetric unit contains four and eight molecules, respectively, with fourfold non-crystallographic symmetry.
Delfosse
Vanessa
V
Laboratoire de Recherche Moléculaire sur les Antibiotiques, INSERM U655, Université Pierre et Marie Curie (Paris 6), CHU Pitié-Salpêtrière, Paris, France.
Hugonnet
Jean Emmanuel
JE
Sougakoff
Wladimir
W
Mayer
Claudine
C
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D016678:Genome; D008970:Molecular Weight; D016366:Open Reading Frames; D046915:Penicillin-Binding Proteins / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D043903:Pyrococcus abyssi / Q000378:metabolism*; D012984:Software; D014961:X-Ray Diffraction; D001618:beta-Lactamases / Q000737:chemistry
D046915:Penicillin-Binding Proteins; D001618:beta-Lactamases