Linked Life Data

9465045

Source:http://linkedlifedata.com/resource/pubmed/id/9465045

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-3-19
pubmed:databankReference
pubmed:abstractText
Paramecium bursaria Chlorella virus PBCV-1 mRNA guanylyl transferase (capping enzyme) has been complexed with an mRNA cap analogue G[5']ppp[5']G and crystallized. The crystals belong to space group C2221 with unit cell dimensions a = 78.4 A, b = 164.1 A, c = 103.3 A, and diffraction data to 3.1 A has been collected by using synchrotron radiation. The structure has been solved by molecular replacement by using each of the two domains in the previously determined structure of the enzyme in complex with GTP. The conformation is open with respect to the active site cleft, and all contacts between enzyme and ligand are mediated by domain 1. One of the guanine bases is bound in the same pocket that is utilized by GTP. The conformation of the ligand positions the beta phosphate and the active site lysine on opposite sides of the alpha phosphate. This geometry is optimal for nucleophilic substitution reactions and has previously been found for GTP in the closed conformational form of the capping enzyme, where the lysine can be guanylylated upon treatment with excess manganese(II) ions. The remainder of the cap analogue runs along the conserved active site Lys82 Thr83 Asp84 Gly85 Ile86 Arg87 motif, and the second guanine, corresponding to the 5' RNA base, is stacked against the hydrophobic Ile86. The ligand displays approximate 2-fold symmetry with intramolecular hydrogen bonding between the 2' and 3' hydroxyls of the two ribose rings.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-15299374, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-3865201, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-5845840, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-6264433, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-7642120, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-7664067, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-7676624, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-7719852, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-7991582, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-8183907, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-8653795, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-875032, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-8757137, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-8794301, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-9160746, http://linkedlifedata.com/resource/pubmed/commentcorrection/9465045-9275164
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0027-8424
pubmed:author
pubmed:issnType
Print
pubmed:day
17
pubmed:volume
95
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1505-10
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Structure of a complex between a cap analogue and mRNA guanylyl transferase demonstrates the structural chemistry of RNA capping.
pubmed:affiliation
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford, OX1 3RE, United Kingdom.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't