Source:http://linkedlifedata.com/resource/pubmed/id/12974386
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
2003-9-16
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pubmed:abstractText |
Ribonuclease (RNase) T1 is a guanyloribonuclease, having two isozymes in nature, Gln25- and Lys25-RNase T1. Between these two isozymes, there is no difference in catalytic activity and three-dimensional structure; however, Lys25-RNase T1 is slightly more stable than Gln25-RNase T1. Recently, it has been suggested that the existence of a salt bridge between Lys25 and Asp29/Glu31 in Lys25-RNase T1 contributes to the stability. To elucidate the effects of the replacement of Lys25 with a Gln on the conformation and microenvironments of RNase T1 in detail, the three-dimensional solution structure of Gln25-RNase T1 was determined by simulated-annealing calculations. As a result, the topology of the overall folding was shown to be very similar to that of the Lys25-isozyme except for some differences. In particular, there were two differences in the property of torsion angles of the two disulfide bonds and the conformations of the residues 11-13, 63-66, and 92-93. With regard to the residues 11-13, the lack of the above-mentioned salt bridge in Gln25-RNase T1 was thought to induce the conformational difference of this segment as compared with the Lys25-isozyme. Furthermore, it was proposed that the perturbation of this segment might transfer to the residues 92-93 via the two disulfide bonds.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamates,
http://linkedlifedata.com/resource/pubmed/chemical/Glycine,
http://linkedlifedata.com/resource/pubmed/chemical/Histidine,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonuclease T1
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1431-6730
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
384
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1173-83
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12974386-Binding Sites,
pubmed-meshheading:12974386-Catalysis,
pubmed-meshheading:12974386-Disulfides,
pubmed-meshheading:12974386-Glutamates,
pubmed-meshheading:12974386-Glycine,
pubmed-meshheading:12974386-Histidine,
pubmed-meshheading:12974386-Hydrogen-Ion Concentration,
pubmed-meshheading:12974386-Lysine,
pubmed-meshheading:12974386-Magnetic Resonance Spectroscopy,
pubmed-meshheading:12974386-Protein Conformation,
pubmed-meshheading:12974386-Ribonuclease T1,
pubmed-meshheading:12974386-Structure-Activity Relationship
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pubmed:year |
2003
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pubmed:articleTitle |
Determination of the NMR structure of Gln25-ribonuclease T1.
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pubmed:affiliation |
Department of Biological Sciences, Faculty of Engineering, Gunma University, Kiryu, Gunma 376-8515, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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