Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2003-5-19
pubmed:abstractText
The ntpK gene of the archaeon Methanopyrus kandleri encodes the equivalent of the c subunit of ATP synthase. The gene product contains 1021 residues and consists of 13 homologous domains, each one corresponding to a single helical hairpin. The amino acid sequence of the domains is highly conserved, ranging between 50 and 80% sequence identity. Each of the 13 domains contains a conserved Gln and Glu residue in the N- and C-terminal helix, respectively, both of which are believed to be involved in cation binding. The protein is likely to form the monomeric rotor of the ATP synthase that consists of 13 hairpin domains.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
543
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
47-50
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
The A-type ATP synthase subunit K of Methanopyrus kandleri is deduced from its sequence to form a monomeric rotor comprising 13 hairpin domains.
pubmed:affiliation
Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN, Haren, The Netherlands. j.s.lolkema@biol.rug.nl
pubmed:publicationType
Journal Article