1l8q
From Proteopedia
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CRYSTAL STRUCTURE OF DNA REPLICATION INITIATION FACTOR
Overview
The initiation of DNA replication is a key event in the cell cycle of all, organisms. In bacteria, replication initiation occurs at specific origin, sequences that are recognized and processed by an oligomeric complex of, the initiator protein DnaA. We have determined the structure of the, conserved core of the Aquifex aeolicus DnaA protein to 2.7 A resolution., The protein comprises an AAA+ nucleotide-binding fold linked through a, long, helical connector to an all-helical DNA-binding domain. The, structure serves as a template for understanding the physical consequences, of a variety of DnaA mutations, and conserved motifs in the protein, suggest how two critical aspects of origin processing, DNA binding and, homo-oligomerization, are mediated. The spatial arrangement of these, motifs in DnaA is similar to that of the eukaryotic-like archaeal, replication initiation factor Cdc6/Orc1, demonstrating that mechanistic, elements of origin processing may be conserved across bacterial, archaeal, and eukaryotic domains of life.
About this Structure
1L8Q is a Single protein structure of sequence from Aquifex aeolicus with MG and ADP as ligands. Full crystallographic information is available from OCA.
Reference
The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation., Erzberger JP, Pirruccello MM, Berger JM, EMBO J. 2002 Sep 16;21(18):4763-73. PMID:12234917
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