8eal
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==SsoMCM hexamer bound to Mg/ADP-BeFx and DNA. Class 1. Merged particles from datasets with 3 different DNA entities== | |
| - | + | <StructureSection load='8eal' size='340' side='right'caption='[[8eal]], [[Resolution|resolution]] 2.34Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8eal]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EAL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EAL FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |
| - | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8eal FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8eal OCA], [https://pdbe.org/8eal PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8eal RCSB], [https://www.ebi.ac.uk/pdbsum/8eal PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8eal ProSAT]</span></td></tr> |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MCM_SACS2 MCM_SACS2] 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: Large Structures]] | ||
| + | [[Category: Saccharolobus solfataricus P2]] | ||
| + | [[Category: Synthetic construct]] | ||
| + | [[Category: Enemark EJ]] | ||
| + | [[Category: Meagher M]] | ||
| + | [[Category: Myasnikov A]] | ||
Revision as of 10:11, 14 December 2022
SsoMCM hexamer bound to Mg/ADP-BeFx and DNA. Class 1. Merged particles from datasets with 3 different DNA entities
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