Structural basis for the activity of a cytoplasmic RNA terminal uridylyl transferase.
Structural basis for the activity of a cytoplasmic RNA terminal uridylyl transferase.
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DOI：
10.1038/nsmb.2329
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发表时间：
2012-08
影响因子：
16.8
通讯作者：
Gilbert, Robert J. C.
中科院分区：
文献类型：
--
作者：
Yates, Luke A.;Fleurdepine, Sophie;Rissland, Olivia S.;De Colibus, Luigi;Harlos, Karl;Norbury, Chris J.;Gilbert, Robert J. C.
Cytoplasmic terminal uridylyltransferases (TUTases) comprise a conserved family of enzymes that negatively regulate the stability or biological activity of a variety of eukaryotic RNAs, including mRNAs and tumor suppressor let-7 miRNAs. Here we describe crystal structures of the Schizosaccharomyces pombe TUTase Cid1 in two Apo conformers and bound to UTP. We demonstrate that a single histidine residue, conserved in mammalian Cid1 orthologs, is responsible for discrimination between UTP and ATP. We also describe a novel high-affinity RNA substrate binding mechanism of Cid1, which is essential for its enzymatic activity and is mediated by three basic patches across the surface of the enzyme. Overall, our structures provide a basis for understanding the activity of Cid1 and a mechanism of UTP selectivity conserved in its human orthologs, with potential implications for anti-cancer drug design.
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DOI：
10.1073/pnas.1003505107
发表时间：
2010-08-24
影响因子：
11.1
作者：
Hamill, Stephanie;Wolin, Sandra L.;Reinisch, Karin M.
通讯作者：
Reinisch, Karin M.
影响因子：
56.9
作者：
SAWAYA, MR;PELLETIER, H;KRAUT, J
通讯作者：
KRAUT, J
影响因子：
56.9
作者：
Bard, J;Zhelkovsky, AM;Bohm, A
通讯作者：
Bohm, A
影响因子：
4.5
作者：
Schmidt, Marie-Joelle;West, Steven;Norbury, Chris J.
通讯作者：
Norbury, Chris J.
影响因子：
5.6
作者：
Stagno, Jason;Aphasizheva, Inna;Aphasizhev, Ruslan
通讯作者：
Aphasizhev, Ruslan