Linked Life Data

9131044

Source:http://linkedlifedata.com/resource/pubmed/id/9131044

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1997-5-22
pubmed:abstractText
In Photosystem I (PS I) the terminal electron acceptors, FA and FB, are iron-sulfur (4Fe-4S) centers, which are bound to the stromal subunit PsaC. The orientation of PsaC is determined relative to the whole PS I complex (see Schubert, W.-D. et al. (1995) in From Light to Biosphere (Mathis, P. ed.), Vol. II, pp. 3-10, Kluwer) from which a molecular model for the structure of PsaC within PS I is derived. Two strategies are followed: (i) PS I single crystal EPR data on the orientation of the g tensors of both FA- and FB- relative to each other and relative to the crystal axes (see preceding paper) are used in conjunction with the central structural part of the bacterial 2 [Fe4S4] ferredoxins, the cysteine binding motifs of which are known to be homologous to those of PsaC; (ii) the same core structure is fitted into the intermediate resolution electron density map of PS I. The PsaC orientation obtained both ways agree well. The local twofold symmetry axis inherent to the ferredoxin model leaves a twofold ambiguity in the structural conclusion. Deviations from this C2-symmetry in the amino acid sequence of PsaC are analyzed with respect to observable properties which would resolve the remaining structural ambiguity. Arguments both for and against FA being the distal iron-sulfur center (to FX) are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
1319
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
199-213
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The structural organization of the PsaC protein in Photosystem I from single crystal EPR and X-ray crystallographic studies.
pubmed:affiliation
Institut für Experimentalphysik, Freie Universität Berlin, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't