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Molecular architecture of SMC proteins and the yeast cohesin complex.
The crystal structure of a bacterial SMC "hinge" region along with EM studies and biochemical experiments on yeast Smc1 and Smc3 proteins show that SMC protamers fold up individually into rod-shaped molecules. Expand
Structure of 20S proteasome from yeast at 2.4Å resolution
Two β-type subunits are processed to an intermediate form, indicating that an additional nonspecific endopeptidase activity may exist which is important for peptide hydrolysis and for the generation of ligands for class I molecules of the major histocompatibility complex. Expand
Bacterial chromosome segregation: structure and DNA binding of the Soj dimer — a conserved biological switch
This analysis shows that dimerisation and activation involving a peptide containing a Lys/Arg is conserved for Soj, ParA and MinD and their modulators Spo0J, ParB and MinE, respectively. Expand
Prokaryotic origin of the actin cytoskeleton
It is demonstrated that the bacterial MreB protein assembles into filaments with a subunit repeat similar to that of F-actin—the physiological polymer of eukaryotic actin, demonstrating that M reB and actin are very similar in three dimensions. Expand
Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.
The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement andExpand
Refined structure of alpha beta-tubulin at 3.5 A resolution.
Details of the tubulin structure such as nucleotide and taxol binding sites, lateral contacts in zinc-sheets, and the significance of the location of highly conserved residues are discussed. Expand
Crystal structure of the bacterial cell-division protein FtsZ
The crystal structure at 2.8 Å resolution of recombinant FtsZ from the hyperthermophilic methanogen Methanococcus jannaschii is reported, which shows a three-dimensional structure similar to the structure of α- and β-tubulin. Expand
Crystal Structure of the Thermosome, the Archaeal Chaperonin and Homolog of CCT
The crystal structure of the thermosome, the archaeal group II chaperonin from T. acidophilum is determined to 2.6 A resolution and Binding of the transition state analog Mg-ADP-AIF3 suggests that the closed conformation corresponds to the ATP form. Expand
Double-stranded DNA translocation: structure and mechanism of hexameric FtsK.
Comparison of FtsK monomer structures from two different crystal forms highlights a conformational change that is the structural basis for a rotary inchworm mechanism of DNA translocation. Expand
Tubulin and FtsZ form a distinct family of GTPases
The highly conserved nucleotide-binding sites of tubulin and FtsZ clearly differ from those of EF-Tu and other GTPases, while resembling the nucleotide site of glyceraldehyde-3-phosphate dehydrogenase, indicating a distinct family of GTP-hydrolyzing proteins. Expand