1w5t: Difference between revisions
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Revision as of 18:21, 5 November 2007
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STRUCTURE OF THE AEROPYRUM PERNIX ORC2 PROTEIN (ADPNP-ADP COMPLEXES)
OverviewOverview
Archaea contain one or more proteins with homology to eukaryotic ORC/Cdc6, proteins. Sequence analysis suggests the existence of at least two, subfamilies of these proteins, for which we propose the nomenclature ORC1, and ORC2. We have determined crystal structures of the ORC2 protein from, the archaeon Aeropyrum pernix in complexes with ADP or a non-hydrolysable, ATP analogue, ADPNP. Between two crystal forms, there are three, crystallographically independent views of the ADP complex and two of the, ADPNP complex. The protein molecules in the three complexes with ADP adopt, very different conformations, while the two complexes with ADPNP are the, same. These structures indicate that there is considerable conformational, flexibility in ORC2 but that ATP binding stabilises a single conformation., We show that the ORC2 protein can bind DNA, and that this activity is, associated with the C-terminal domain of the protein. We present a model, for the interaction of the winged helix (WH) domain of ORC2 with DNA that, differs from that proposed previously for Pyrobaculum aerophilum ORC/Cdc6.
About this StructureAbout this Structure
1W5T is a Single protein structure of sequence from Aeropyrum pernix with MG, ANP and ADP as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
Conformational changes induced by nucleotide binding in Cdc6/ORC from Aeropyrum pernix., Singleton MR, Morales R, Grainge I, Cook N, Isupov MN, Wigley DB, J Mol Biol. 2004 Oct 22;343(3):547-57. PMID:15465044
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