Journal
RNA
Volume 20, Issue 10, Pages 1560-1566Publisher
COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
DOI: 10.1261/rna.045823.114
Keywords
RtcA; RNA 3 '-phosphate termini; 2 ',3 '-cyclic phosphate termini
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Funding
- National Institutes of Health (NIH) [F32 GM100681, U01 GM098248, R01 CA073808]
- US Department of Energy (DOE) [DE-AC02-06CH11357]
- [Y1-CO-1020]
- [Y1-GM-1104]
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RNA 3'-phosphate cyclase (RtcA) catalyzes the ATP-dependent cyclization of a 3'-phosphate to form a 2',3'-cyclic phosphate at RNA termini. Cyclization proceeds through RtcA AMP and RNA(3')pp(5')A covalent intermediates, which are analogous to intermediates formed during catalysis by the tRNA ligase RtcB. Here we present a crystal structure of Pyrococcus horikoshii RtcA in complex with a 3'-phosphate terminated RNA and adenosine in the AMP-binding pocket. Our data reveal that RtcA recognizes substrate RNA by ensuring that the terminal 3'-phosphate makes a large contribution to RNA binding. Furthermore, the RNA 3'-phosphate is poised for in-line attack on the P-N bond that links the phosphorous atom of AMP to N-epsilon of His307. Thus, we provide the first insights into RNA 3'-phosphate termini recognition and the mechanism of 3'-phosphate activation by an Rtc enzyme.
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