pubmed-article:1917989 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1917989 | lifeskim:mentions | umls-concept:C0752021 | lld:lifeskim |
pubmed-article:1917989 | lifeskim:mentions | umls-concept:C0026383 | lld:lifeskim |
pubmed-article:1917989 | lifeskim:mentions | umls-concept:C0205409 | lld:lifeskim |
pubmed-article:1917989 | lifeskim:mentions | umls-concept:C0062713 | lld:lifeskim |
pubmed-article:1917989 | lifeskim:mentions | umls-concept:C2699488 | lld:lifeskim |
pubmed-article:1917989 | pubmed:issue | 28 | lld:pubmed |
pubmed-article:1917989 | pubmed:dateCreated | 1991-11-8 | lld:pubmed |
pubmed-article:1917989 | pubmed:abstractText | The molecular structure of a high potential iron-sulfur protein (HiPIP) isolated from the purple photosynthetic bacterium, Ectothiorhodospira halophila strain BN9626, has been solved by x-ray diffraction analysis to a nominal resolution of 2.5 A and refined to a crystallographic R value of 18.4% including all measured x-ray data from 30.0- to 2.5-A resolution. Crystals used in the investigation contained two molecules/asymmetric unit and belonged to the space group P21 with unit cell dimensions of a = 60.00 A, b = 31.94 A, c = 40.27 A, and beta = 100.5 degrees. An interpretable electron density map, obtained by combining x-ray data from one isomorphous heavy atom derivative with non-crystallographic symmetry averaging and solvent flattening, clearly showed that this high potential iron-sulfur protein contains 71 amino acid residues, rather than 70 as originally reported. As in other bacterial ferredoxins, the [4Fe-4S] cluster adopts a cubane-like conformation and is ligated to the protein via four cysteinyl sulfur ligands. The overall secondary structure of the E. halophila HiPIP is characterized by a series of Type I and Type II turns allowing the polypeptide chain to wrap around the [4Fe-4S] prosthetic group. The hydrogen bonding pattern around the cluster is nearly identical to that originally observed in the 85-amino acid residue Chromatium vinosum HiPIP and consequently, the 240 mV difference in redox potentials between these two proteins cannot be simply attributed to hydrogen bonding patterns alone. | lld:pubmed |
pubmed-article:1917989 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1917989 | pubmed:language | eng | lld:pubmed |
pubmed-article:1917989 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1917989 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1917989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1917989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1917989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1917989 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1917989 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1917989 | pubmed:month | Oct | lld:pubmed |
pubmed-article:1917989 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:1917989 | pubmed:author | pubmed-author:MeyerT ETE | lld:pubmed |
pubmed-article:1917989 | pubmed:author | pubmed-author:RaymentII | lld:pubmed |
pubmed-article:1917989 | pubmed:author | pubmed-author:HoldenH MHM | lld:pubmed |
pubmed-article:1917989 | pubmed:author | pubmed-author:BreiterD RDR | lld:pubmed |
pubmed-article:1917989 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1917989 | pubmed:day | 5 | lld:pubmed |
pubmed-article:1917989 | pubmed:volume | 266 | lld:pubmed |
pubmed-article:1917989 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1917989 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1917989 | pubmed:pagination | 18660-7 | lld:pubmed |
pubmed-article:1917989 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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pubmed-article:1917989 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1917989 | pubmed:articleTitle | The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution. | lld:pubmed |
pubmed-article:1917989 | pubmed:affiliation | Department of Chemistry, University of Wisconsin, Madison 53705. | lld:pubmed |
pubmed-article:1917989 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1917989 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:1917989 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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