The structure of porin from Paracoccus denitrificans at 3.1 A resolution. 1997

A Hirsch, and J Breed, and K Saxena, and O M Richter, and B Ludwig, and K Diederichs, and W Welte
Universität Konstanz, Fakultät für Biologie, Germany.

The crystal structure of a non-specific porin from Paracoccus denitrificans at 3.1 A resolution has been solved by molecular replacement using the porin from Rhodopseudomonas blastica as the search model. Paracoccus porin is very similar to other non-specific porins of known structure: a trimer of 16 stranded beta-barrels each with a central pore constricted by a long extracellular loop folding back against the barrel wall. The distinctive distribution of charged residues of this non-specific porin contributes to understanding the relation between structure and ion selectivity.

UI MeSH Term Description Entries
D008958 Models, Molecular Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures. Molecular Models,Model, Molecular,Molecular Model
D010231 Paracoccus denitrificans A species of bacteria isolated from soil. Micrococcus denitrificans
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D012241 Rhodopseudomonas A genus of gram-negative, rod-shaped, phototrophic bacteria found in aquatic environments. Internal photosynthetic membranes are present as lamellae underlying the cytoplasmic membrane.
D017433 Protein Structure, Secondary The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to ALPHA-HELICES; BETA-STRANDS (which align to form BETA-SHEETS), or other types of coils. This is the first folding level of protein conformation. Secondary Protein Structure,Protein Structures, Secondary,Secondary Protein Structures,Structure, Secondary Protein,Structures, Secondary Protein
D018272 Porins Porins are protein molecules that were originally found in the outer membrane of GRAM-NEGATIVE BACTERIA and that form multi-meric channels for the passive DIFFUSION of WATER; IONS; or other small molecules. Porins are present in bacterial CELL WALLS, as well as in plant, fungal, mammalian and other vertebrate CELL MEMBRANES and MITOCHONDRIAL MEMBRANES. Pore Protein,Pore Proteins,Porin,Protein, Pore,Proteins, Pore
D018360 Crystallography, X-Ray The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) X-Ray Crystallography,Crystallography, X Ray,Crystallography, Xray,X Ray Crystallography,Xray Crystallography,Crystallographies, X Ray,X Ray Crystallographies

Related Publications

A Hirsch, and J Breed, and K Saxena, and O M Richter, and B Ludwig, and K Diederichs, and W Welte
April 1985, Journal of bacteriology,
A Hirsch, and J Breed, and K Saxena, and O M Richter, and B Ludwig, and K Diederichs, and W Welte
August 1995, Nature,
A Hirsch, and J Breed, and K Saxena, and O M Richter, and B Ludwig, and K Diederichs, and W Welte
July 2006, Biopolymers,
A Hirsch, and J Breed, and K Saxena, and O M Richter, and B Ludwig, and K Diederichs, and W Welte
July 1996, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
A Hirsch, and J Breed, and K Saxena, and O M Richter, and B Ludwig, and K Diederichs, and W Welte
January 2003, The Biochemical journal,
A Hirsch, and J Breed, and K Saxena, and O M Richter, and B Ludwig, and K Diederichs, and W Welte
February 1998, Journal of molecular biology,
A Hirsch, and J Breed, and K Saxena, and O M Richter, and B Ludwig, and K Diederichs, and W Welte
July 1996, Acta crystallographica. Section D, Biological crystallography,
A Hirsch, and J Breed, and K Saxena, and O M Richter, and B Ludwig, and K Diederichs, and W Welte
September 2003, Acta crystallographica. Section D, Biological crystallography,
A Hirsch, and J Breed, and K Saxena, and O M Richter, and B Ludwig, and K Diederichs, and W Welte
May 1993, Protein science : a publication of the Protein Society,
A Hirsch, and J Breed, and K Saxena, and O M Richter, and B Ludwig, and K Diederichs, and W Welte
April 1997, European journal of biochemistry,
Copied contents to your clipboard!