| pubmed-article:11372197 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11372197 | lifeskim:mentions | umls-concept:C0995425 | lld:lifeskim |
| pubmed-article:11372197 | lifeskim:mentions | umls-concept:C0010798 | lld:lifeskim |
| pubmed-article:11372197 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:11372197 | lifeskim:mentions | umls-concept:C0392756 | lld:lifeskim |
| pubmed-article:11372197 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:11372197 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:11372197 | pubmed:dateCreated | 2001-5-24 | lld:pubmed |
| pubmed-article:11372197 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11372197 | pubmed:abstractText | Cytochrome c554 (cyt c554) is a tetra-heme cytochrome involved in the oxidation of NH3 by Nitrosomonas europaea. The X-ray crystal structures of both the oxidized and dithionite-reduced states of cyt c554 in a new, rhombohedral crystal form have been solved by molecular replacement, at 1.6 A and 1.8 A resolution, respectively. Upon reduction, the conformation of the polypeptide chain changes between residues 175 and 179, which are adjacent to hemes III and IV. Cyt c554 displays conserved heme-packing motifs that are present in other heme-containing proteins. Comparisons to hydroxylamine oxidoreductase, the electron donor to cyt c554, and cytochrome c nitrite reductase, an enzyme involved in nitrite ammonification, reveal substantial structural similarity in the polypeptide chain surrounding the heme core environment. The structural determinants of these heme-packing motifs extend to the buried water molecules that hydrogen bond to the histidine ligands to the heme iron. In the original structure determination of a tetragonal crystal form, a cis peptide bond between His129 and Phe130 was identified that appeared to be stabilized by crystal contacts. In the rhombohedral crystal form used in the present high-resolution structure determination, this peptide bond adopts the trans conformation, but with disallowed angles of phi and psi. | lld:pubmed |
| pubmed-article:11372197 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11372197 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11372197 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11372197 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11372197 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11372197 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11372197 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11372197 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11372197 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11372197 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11372197 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:11372197 | pubmed:issn | 0949-8257 | lld:pubmed |
| pubmed-article:11372197 | pubmed:author | pubmed-author:HooperA BAB | lld:pubmed |
| pubmed-article:11372197 | pubmed:author | pubmed-author:ReesD CDC | lld:pubmed |
| pubmed-article:11372197 | pubmed:author | pubmed-author:ArcieroD MDM | lld:pubmed |
| pubmed-article:11372197 | pubmed:author | pubmed-author:IversonT MTM | lld:pubmed |
| pubmed-article:11372197 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11372197 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:11372197 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11372197 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11372197 | pubmed:pagination | 390-7 | lld:pubmed |
| pubmed-article:11372197 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:11372197 | pubmed:meshHeading | pubmed-meshheading:11372197... | lld:pubmed |
| pubmed-article:11372197 | pubmed:meshHeading | pubmed-meshheading:11372197... | lld:pubmed |
| pubmed-article:11372197 | pubmed:meshHeading | pubmed-meshheading:11372197... | lld:pubmed |
| pubmed-article:11372197 | pubmed:meshHeading | pubmed-meshheading:11372197... | lld:pubmed |
| pubmed-article:11372197 | pubmed:meshHeading | pubmed-meshheading:11372197... | lld:pubmed |
| pubmed-article:11372197 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:11372197 | pubmed:articleTitle | High-resolution structures of the oxidized and reduced states of cytochrome c554 from Nitrosomonas europaea. | lld:pubmed |
| pubmed-article:11372197 | pubmed:affiliation | Division of Chemistry and Chemical Engineering and Howard Hughes Medical Institute, MC 147-75 CH, California Institute of Technology, Pasadena, CA 91125, USA. | lld:pubmed |
| pubmed-article:11372197 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11372197 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:11372197 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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