Crystal structure of a small heat-shock protein
Article Abstract:
Investigation of the crystal structure of a small heat-shock protein from Methanococcus jannaschii, a hyperthermophilic archaeon, reveals a monomeric folding unit which is a composite beta-sandwich. Within this structure, one of the beta-strands comes from a neighbouring molecule. A hollow spherical complex of octahedral symmetry is created from 24 monomers. There are many possible mechanisms to explain why small heat-shock proteins are able to protect other proteins from denaturation. These include the fact that certain proteins or RNAs vital for the cells' survival under stress could get trapped in or on the outer surface of the spheres during in vivo assembly of the hollow spheres.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Electron transfer by domain movement in cytochrome bc1
Article Abstract:
It has been established that the extrinsic domain of the Rieske protein containing the iron-sulphur cluster in cytochrome bc1, one of the three main respiratory enzyme complexes present in the inner mitochondrial membrane, assumes one of two conformations in the complexes. In one conformation, the iron-sulphur cluster is close to its electron acceptor, the haem group of cytochrome c1, but distant from the assumed binding site of its electron donor, ubiquinol, in cytochrome b. In the other, the cluster is closer to cytochrome b and further away from cytochrome c1. It was possible to identify the binding sites for two Qo-site inhibitors, stigmatellin and myxothiazol.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Crystal structure of the ATP-binding subunit of an ABC transporter
Article Abstract:
ABC transporters have four structural domains, two nucelotide-binding domains and two transmembrane domains. The Escherichia coli genome sequence shows that the largest family of paralogous E. coli proteins consist of ABC transporters. The crystal structure of HisP, an ATP-binding subunit of the ABC transporter histidine permease from Salmonella typhimurium, is reported, providing a base for understanding the properties of ABC transporters and defective cystic fibrosis transmembrane conductance regulator (CFTR) proteins.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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