2v1u
From Proteopedia
STRUCTURE OF THE AEROPYRUM PERNIX ORC1 PROTEIN IN COMPLEX WITH DNA
Structural highlights
FunctionCDC61_AERPE Involved in regulation of DNA replication (By similarity). Binds DNA.[HAMAP-Rule:MF_01407][1] 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 PubMedDNA replication in archaea and in eukaryotes share many similarities. We report the structure of an archaeal origin recognition complex protein, ORC1, bound to an origin recognition box, a DNA sequence that is found in multiple copies at replication origins. DNA binding is mediated principally by a C-terminal winged helix domain that inserts deeply into the major and minor grooves, widening them both. However, additional DNA contacts are made with the N-terminal AAA+ domain, which inserts into the minor groove at a characteristic G-rich sequence, inducing a 35 degrees bend in the duplex and providing directionality to the binding site. Both contact regions also induce substantial unwinding of the DNA. The structure provides insight into the initial step in assembly of a replication origin and recruitment of minichromosome maintenance (MCM) helicase to that origin. Structural basis of DNA replication origin recognition by an ORC protein.,Gaudier M, Schuwirth BS, Westcott SL, Wigley DB Science. 2007 Aug 31;317(5842):1213-6. PMID:17761880[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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