Linked Life Data

17642515

Source:http://linkedlifedata.com/resource/pubmed/id/17642515

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 8
pubmed:dateCreated
2007-7-23
pubmed:abstractText
The biotin carboxylase (BC) domain of pyruvate carboxylase (PC) from Bacillus thermodenitrificans (BC-bPC) was crystallized in an orthorhombic form (space group P2(1)2(1)2(1)), with unit-cell parameters a = 79.6, b = 116.0, c = 115.7 A. Two BC protomers are contained in the asymmetric unit. Diffraction data were collected at 100 K and the crystal structure was solved by the molecular-replacement method and refined against reflections in the 20.0-2.4 A resolution range, giving an R factor of 0.235 and a free R factor of 0.292. The overall structure of BC-bPC is similar to those of the BC subunits of Aquifex aeolicus PC (BC-aPC) and Escherichia coli ACC (BC-eACC). The crystal structure revealed that BC-bPC forms a unique dimeric quaternary structure, which might be caused as a result of the division of the BC domain from the rest of the protein. The position of domain B in BC-bPC differs from those in other enzymes of similar structure (BC-aPC and BC-eACC).
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
885-90
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans.
pubmed:affiliation
ZOEGENE Corporation, Aoba, Yokohama 227-8502, Japan. kondo@bio.kyutech.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't