17142895

Source:http://linkedlifedata.com/resource/pubmed/id/17142895

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0032589, umls-concept:C0205242, umls-concept:C0376315, umls-concept:C0678594, umls-concept:C1017746, umls-concept:C2699488
pubmed:issue	Pt 12
pubmed:dateCreated	2006-12-4
pubmed:databankReference	http://linkedlifedata.com/resource/pubmed/xref/PDB/1VGJ, http://linkedlifedata.com/resource/pubmed/xref/PDB/R1VGJSF
pubmed:abstractText	Bacterial and archaeal 2'-5' RNA ligases, members of the 2H phosphoesterase superfamily, catalyze the linkage of the 5' and 3' exons via a 2'-5'-phosphodiester bond during tRNA-precursor splicing. The crystal structure of the 2'-5' RNA ligase PH0099 from Pyrococcus horikoshii OT3 was solved at 1.94 A resolution (PDB code 1vgj). The molecule has a bilobal alpha+beta arrangement with two antiparallel beta-sheets constituting a V-shaped active-site cleft, as found in other members of the 2H phosphoesterase superfamily. The present structure was significantly different from that determined previously at 2.4 A resolution (PDB code 1vdx) in the active-site cleft; the entrance to the cleft is wider and the active site is easily accessible to the substrate (RNA precursor) in our structure. Structural comparison with the 2'-5' RNA ligase from Thermus thermophilus HB8 also revealed differences in the RNA precursor-binding region. The structural differences in the active-site residues (tetrapeptide motifs H-X-T/S-X) between the members of the 2H phosphoesterase superfamily are discussed.
pubmed:commentsCorrections	http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-10734185, http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-11080166, http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-11694509, http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-12466548, http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-12798681, http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-12933796, http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-12947117, http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-15713463, http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-15923379, http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-2207062, http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-6186398, http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-9582290, http://linkedlifedata.com/resource/pubmed/commentcorrection/17142895-9757107
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101226117
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Polynucleotide Ligases
pubmed:status	MEDLINE
pubmed:month	Dec
pubmed:issn	1744-3091
pubmed:author	pubmed-author:GaoYong-GuiYG, pubmed-author:KenY HYH, pubmed-author:OkadaAyukoA, pubmed-author:TanakaIsaoI
pubmed:issnType	Electronic
pubmed:day	1
pubmed:volume	62
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1196-200
pubmed:dateRevised	2009-11-18
pubmed:meshHeading	pubmed-meshheading:17142895-Crystallization, pubmed-meshheading:17142895-Crystallography, X-Ray, pubmed-meshheading:17142895-Models, Molecular, pubmed-meshheading:17142895-Polynucleotide Ligases, pubmed-meshheading:17142895-Pyrococcus horikoshii
pubmed:year	2006
pubmed:articleTitle	The structure of Pyrococcus horikoshii 2'-5' RNA ligase at 1.94 A resolution reveals a possible open form with a wider active-site cleft.
pubmed:affiliation	Faculty of Advanced Life Sciences, Graduate School of Life Sciences, Hokkaido University, Sapporo 060-0810, Japan.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't