Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1985-5-14
pubmed:abstractText
The mother enzyme of RNase T1 was co-crystallized with its natural product, 3'-GMP at pH 4.0. The X-ray structure of this complex was refined with 2432 reflections in the 5.4-2.6 A range using a stereochemical restrained method (conventional R = 27.4%). The overall polypeptide chain folding is very similar in the secondary structure elements to the RNase T1 in the complex with 2'-GMP crystallized also at pH 4.0, but larger conformational changes occur in the loop regions. The base recognition scheme is identical in both complexes but in RNase T1 X 3'-GMP, the ribose phosphate is not seen in the electron density, probably due to static disorder.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
183
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
115-8
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
Three-dimensional structure of the ribonuclease T1 X 3'-guanylic acid complex at 2.6 A resolution.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't