TY  - JOUR
A1  - Ihle, Yvonne
A1  - Ohlenschläger, Oliver
A1  - Häfner, Sabine
A1  - Duchardt-Ferner, Elke
A1  - Zacharias, Martin
A1  - Seitz, Simone
A1  - Zell, Roland
A1  - Ramachandran, Ramadurai
A1  - Görlach, Matthias
T1  - A novel cGUUAg tetraloop structure with a conserved yYNMGg-type backbone conformation from cloverleaf 1 of bovine enterovirus 1 RNA
T2  - Nucleic acids research
N2  - The 5'-terminal cloverleaf (CL)-like RNA structures are essential for the initiation of positive- and negative-strand RNA synthesis of entero- and rhinoviruses. SLD is the cognate RNA ligand of the viral proteinase 3C (3Cpro), which is an indispensable component of the viral replication initiation complex. The structure of an 18mer RNA representing the apical stem and the cGUUAg D-loop of SLD from the first 5'-CL of BEV1 was determined in solution to a root-mean-square deviation (r.m.s.d.) (all heavy atoms) of 0.59 A (PDB 1Z30). The first (antiG) and last (synA) nucleotide of the D-loop forms a novel ‘pseudo base pair’ without direct hydrogen bonds. The backbone conformation and the base-stacking pattern of the cGUUAg-loop, however, are highly similar to that of the coxsackieviral uCACGg D-loop (PDB 1RFR) and of the stable cUUCGg tetraloop (PDB 1F7Y) but surprisingly dissimilar to the structure of a cGUAAg stable tetraloop (PDB 1MSY), even though the cGUUAg BEV D-loop and the cGUAAg tetraloop differ by 1 nt only. Together with the presented binding data, these findings provide independent experimental evidence for our model [O. Ohlenschläger, J. Wöhnert, E. Bucci, S. Seitz, S. Häfner, R. Ramachandran, R. Zell and M. Görlach (2004) Structure, 12, 237–248] that the proteinase 3Cpro recognizes structure rather than sequence.
Y1  - 2006
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/2812
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30-26030
SN  - 1362-4962
SN  - 0305-1048
N1  - © The Author 2005. Published by Oxford University Press. All rights reserved
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VL  - 33
IS  - 6
SP  - 2003
EP  - 2011
PB  - Oxford Univ. Press
CY  - Oxford
ER  -