4fdg
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| - | {{STRUCTURE_4fdg| PDB=4fdg | SCENE= }} | ||
| - | ===Crystal Structure of an Archaeal MCM Filament=== | ||
| - | {{ABSTRACT_PUBMED_23361460}} | ||
| - | == | + | ==Crystal Structure of an Archaeal MCM Filament== |
| - | [[http://www.uniprot.org/uniprot/ | + | <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> | |
| - | <references | + | </table> |
| - | [[Category: | + | == Function == |
| - | [[Category: | + | [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> |
| - | [[Category: Brewster | + | == References == |
| - | [[Category: Chen | + | <references/> |
| - | [[Category: Fu | + | __TOC__ |
| - | [[Category: Slaymaker | + | </StructureSection> |
| - | + | [[Category: Large Structures]] | |
| + | [[Category: Saccharolobus solfataricus]] | ||
| + | [[Category: Brewster AB]] | ||
| + | [[Category: Chen XS]] | ||
| + | [[Category: Fu Y]] | ||
| + | [[Category: Slaymaker IM]] | ||
Current revision
Crystal Structure of an Archaeal MCM Filament
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