2m45: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [http://www.ebi.ac.uk/pdbsum/2m45 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2m45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m45 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m45 RCSB], [http://www.ebi.ac.uk/pdbsum/2m45 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/MCM_SULSO MCM_SULSO]] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.<ref>PMID:11821426</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 19:20, 24 December 2014
NMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricusNMR solution structure of the C-terminus of the minichromosome maintenance protein MCM from Sulfolobus solfataricus
Structural highlights
Function[MCM_SULSO] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.[1] References
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