1l2m

Minimized Average Structure of the N-terminal, DNA-binding domain of the replication initiation protein from a geminivirus (Tomato yellow leaf curl virus-Sardinia)Minimized Average Structure of the N-terminal, DNA-binding domain of the replication initiation protein from a geminivirus (Tomato yellow leaf curl virus-Sardinia)

Structural highlights 1l2m is a 1 chain structure with sequence from Tomato yellow leaf curl sardinia virus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1l5i Gene: rep (Tomato yellow leaf curl Sardinia virus) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1l2m, 1 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image