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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-5-6
pubmed:databankReference
pubmed:abstractText
In the second step of the two consecutive transesterifications of the self-splicing reaction of the group I intron, the conserved guanosine at the 3' terminus of the intron (omegaG) binds to the guanosine-binding site (GBS) in the intron. In the present study, we designed a 22-nt model RNA (GBS/omegaG) including the GBS and omegaG from the Tetrahymena group I intron, and determined the solution structure by NMR methods. In this structure, omegaG is recognized by the formation of a base triple with the G264 x C311 base pair, and this recognition is stabilized by the stacking interaction between omegaG and C262. The bulged structure at A263 causes a large helical twist angle (40 +/- 80) between the G264 x C311 and C262 x G312 base pairs. We named this type of binding pocket with a bulge and a large twist, formed on the major groove, a "Bulge-and-Twist" (BT) pocket. With another twist angle between the C262 x G312 and G413 x C313 base pairs (45 +/- 100), the axis of GBS/omegaG is kinked at the GBS region. This kinked axis superimposes well on that of the corresponding region in the structure model built on a 5.0 A resolution electron density map (Golden et al., Science, 1998, 282:345-358). This compact structure of the GBS is also consistent with previous biochemical studies on group I introns. The BT pockets are also found in the arginine-binding site of the HIV-TAR RNA, and within the 16S rRNA and the 23S rRNA.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-10024168, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-10074469, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-10388561, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-10500151, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-10535916, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-10736224, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-10937989, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-11014182, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-1315076, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-1377367, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-1381347, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-1613800, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-1621097, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-1700131, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-1706937, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-1709522, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-1762161, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-2017681, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-2258934, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-2431151, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-2653441, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-2685606, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-3072260, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-3381099, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-8219742, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-8284214, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-8421499, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-8614639, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-8781224, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-9000010, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-9000624, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-9092663, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-9126842, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-9254623, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-9285596, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-9582093, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-9644241, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-9753434, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-9841391, http://linkedlifedata.com/resource/pubmed/commentcorrection/11991639-9846872
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1355-8382
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
440-51
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Solution structure of an RNA fragment with the P7/P9.0 region and the 3'-terminal guanosine of the tetrahymena group I intron.
pubmed:affiliation
Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Comparative Study
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