Linked Life Data

20833871

Source:http://linkedlifedata.com/resource/pubmed/id/20833871

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2011-1-5
pubmed:abstractText
Eukaryotic ATP-dependent 6-phosphofructokinases (Pfks) differ from their bacterial counterparts in a much more complex structural organization and allosteric regulation. Pichia pastoris Pfk (PpPfk) is, with ? 1 MDa, the most complex and probably largest eukaryotic Pfk. We have determined the crystal structure of full-length PpPfk to 3.05 ? resolution in the T state. PpPfk forms a (???)(4) dodecamer of D(2) symmetry with dimensions of 161 × 157 × 233 ? mainly via interactions of the ? chains. The N-terminal domains of the ? and ? chains have folds that are distantly related to glyoxalase I, but the active sites are no longer functional. Interestingly, these domains located at the 2 distal ends of this protein along the long 2-fold axis form a (??)(2) dimer as does the core Pfk domains; however, the domains are swapped across the tetramerization interface. In PpPfk, the unique ? subunit participates in oligomerization of the ?? chains. This modulator protein was acquired from an ancient S-adenosylmethionine-dependent methyltransferase. The identification of novel ATP binding sites, which do not correspond to the bacterial catalytic or effector binding sites, point to marked structural and functional differences between bacterial and eukaryotic Pfks.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1530-6860
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
89-98
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Molecular architecture and structural basis of allosteric regulation of eukaryotic phosphofructokinases.
pubmed:affiliation
Institute of Bioanalytical Chemistry, Center for Biotechnology and Biomedicine, University of Leipzig, Deutscher Platz 5, 04103 Leipzig, Germany. strater@bbz.uni-leipzig.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't