6mii: Difference between revisions
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The | ==Crystal structure of minichromosome maintenance protein MCM/DNA complex== | ||
<StructureSection load='6mii' size='340' side='right'caption='[[6mii]], [[Resolution|resolution]] 3.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6mii]] is a 7 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MII OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MII FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=08T:[[[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-BIS(OXIDANYL)OXOLAN-2-YL]METHOXY-OXIDANYL-PHOSPHORYL]OXY-OXIDANYL-PHOSPHORYL]OXY-TRIS(FLUORANYL)BERYLLIUM'>08T</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
[[Category: | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA_helicase DNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.12 3.6.4.12] </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=6mii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mii OCA], [http://pdbe.org/6mii PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mii RCSB], [http://www.ebi.ac.uk/pdbsum/6mii PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mii ProSAT]</span></td></tr> | |||
</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__ | |||
</StructureSection> | |||
[[Category: DNA helicase]] | |||
[[Category: Large Structures]] | |||
[[Category: Enemark, E J]] | |||
[[Category: Epling, L B]] | |||
[[Category: Meagher, M]] | |||
[[Category: Aaa+]] | |||
[[Category: Dna]] | |||
[[Category: Helicase]] | |||
[[Category: Hydrolase-dna complex]] | |||
[[Category: Mcm]] | |||