4fdg: Difference between revisions
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New page: '''Unreleased structure''' The entry 4fdg is ON HOLD Authors: Slaymaker, I.M., Fu, Y., Brewster, A.B., Chen, X.S Description: Structure of Replication Factor X |
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==Crystal Structure of an Archaeal MCM Filament== | |||
<StructureSection load='4fdg' size='340' side='right'caption='[[4fdg]], [[Resolution|resolution]] 4.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4fdg]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FDG FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.1Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4fdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fdg OCA], [https://pdbe.org/4fdg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fdg RCSB], [https://www.ebi.ac.uk/pdbsum/4fdg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fdg 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]] | |||
[[Category: Brewster AB]] | |||
[[Category: Chen XS]] | |||
[[Category: Fu Y]] | |||
[[Category: Slaymaker IM]] | |||
Latest revision as of 14:15, 1 March 2024
Crystal Structure of an Archaeal MCM FilamentCrystal Structure of an Archaeal MCM Filament
Structural highlights
FunctionMCM_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.[1] References
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