Linked Life Data

6631958

Source:http://linkedlifedata.com/resource/pubmed/id/6631958

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1983-12-17
pubmed:abstractText
The thermolabile glyceraldehyde-3-phosphate dehydrogenase from the facultative thermophile Bacillus coagulans has a crystallographically exact 2-fold rotation axis of symmetry in one of its orthorhombic crystal forms (Lee et al., 1982). Using various crystallographic techniques, we have now identified this axis to be the molecular R-axis, which is the symmetry axis that relates the two subunits that form each active site of the tetrameric enzyme. This is in contrast to the symmetry of the human skeletal muscle enzyme wherein the crystallographically exact axis was found to be the Q-axis (Buehner et al., 1974). This finding could have important implications for the possible mechanism for the allosteric behavior of this molecule.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
169
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
963-74
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Molecular symmetry of glyceraldehyde-3-phosphate dehydrogenase from Bacillus coagulans.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't