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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1985-5-14
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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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
183
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
115-8
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:2984048-5'-Guanylic Acid,
pubmed-meshheading:2984048-Chemistry, Physical,
pubmed-meshheading:2984048-Endoribonucleases,
pubmed-meshheading:2984048-Guanine Nucleotides,
pubmed-meshheading:2984048-Models, Molecular,
pubmed-meshheading:2984048-Physicochemical Phenomena,
pubmed-meshheading:2984048-Protein Conformation,
pubmed-meshheading:2984048-Ribonuclease T1,
pubmed-meshheading:2984048-X-Ray Diffraction
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pubmed:year |
1985
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pubmed:articleTitle |
Three-dimensional structure of the ribonuclease T1 X 3'-guanylic acid complex at 2.6 A resolution.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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