3f9v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 6: Line 6:
<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=3f9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3f9v RCSB], [http://www.ebi.ac.uk/pdbsum/3f9v 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=3f9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f9v OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3f9v RCSB], [http://www.ebi.ac.uk/pdbsum/3f9v 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>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 11:07, 25 December 2014

Crystal Structure Of A Near Full-Length Archaeal MCM: Functional Insights For An AAA+ Hexameric Helicase

3f9v, resolution 4.35Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools