Crystallization and preliminary X-ray analysis of a cohesin-like module from AF2375 of the archaeon Archaeoglobus fulgidus.
A cohesin-like module of 160 amino-acid residues from the hypothetical protein AF2375 of the noncellulolytic, hyperthermophilic, sulfate-reducing archaeon Archaeoglobus fulgidus was cloned, expressed, purified, crystallized and subjected to X-ray structural study in order to compare its structure with those of cellulolytic cohesins. The crystals had cubic symmetry, with unit-cell parameters a = b = c = 101.75 A in space group P4(3)32, and diffracted to 1.82 A resolution. The asymmetric unit contained a single cohesin molecule. A model assembled from six cohesin structures (PDB entries 1anu, 1aoh, 1g1k, 1qzn, 1zv9 and 1tyj) of very low sequence identity to the cohesin-like module was used in molecular-replacement attempts, producing a marginal solution.
Voronov-Goldman
Milana
M
Department of Molecular Microbiology and Biotechnology, Tel Aviv University, Israel.
Noach
Ilit
I
Lamed
Raphael
R
Shimon
Linda J W
LJ
Borovok
Ilya
I
Bayer
Edward A
EA
Frolow
Felix
F
D019843:Archaeal Proteins / Q000737:chemistry*; D019611:Archaeoglobus fulgidus / Q000737:chemistry*; D018797:Cell Cycle Proteins / Q000737:chemistry*; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D000097722:Cohesins
D019843:Archaeal Proteins; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D000097722:Cohesins