1l2m
From Proteopedia
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Minimized Average Structure of the N-terminal, DNA-binding domain of the replication initiation protein from a geminivirus (Tomato yellow leaf curl virus-Sardinia)
Overview
Rolling circle replication is a mechanism for copying single-stranded, genomes by means of double-stranded intermediates. A multifunctional, replication initiator protein (Rep) is indispensable for the precise, initiation and termination of this process. Despite the ubiquitous, presence and fundamental importance of rolling circle replication, elements, structural information on their respective replication, initiators is still missing. Here we present the solution NMR structure of, the catalytic domain of Rep, the initiator protein of tomato yellow leaf, curl virus. It is composed of a central five-stranded anti-parallel, beta-sheet, flanked by a small two-stranded beta-sheet, a beta-hairpin and, two alpha-helices. Surprisingly, the structure reveals that the catalytic, Rep domain is related to a large group of proteins that bind RNA or DNA., Identification of Rep as resembling the family of, ribonucleoprotein/RNA-recognition motif fold proteins establishes a, structure-based evolutionary link between RNA binding proteins, splicing, factors, and replication initiators of prokaryotic and eukaryotic, single-stranded DNA elements and mammalian DNA tumor viruses.
About this Structure
1L2M is a Single protein structure of sequence from Tomato yellow leaf curl sardinia virus. Full crystallographic information is available from OCA.
Reference
The structure of a replication initiator unites diverse aspects of nucleic acid metabolism., Campos-Olivas R, Louis JM, Clerot D, Gronenborn B, Gronenborn AM, Proc Natl Acad Sci U S A. 2002 Aug 6;99(16):10310-5. Epub 2002 Jul 18. PMID:12130667
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