1w5t: Difference between revisions
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<StructureSection load='1w5t' size='340' side='right'caption='[[1w5t]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1w5t' size='340' side='right'caption='[[1w5t]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1w5t]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1w5t]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aerpx Aerpx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W5T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W5T FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1w5s|1w5s]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1w5s|1w5s]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1w5t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w5t OCA], [https://pdbe.org/1w5t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w5t RCSB], [https://www.ebi.ac.uk/pdbsum/1w5t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w5t ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CDC62_AERPE CDC62_AERPE]] Involved in regulation of DNA replication (By similarity). Binds DNA.[HAMAP-Rule:MF_01407]<ref>PMID:15465044</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 16:32, 13 October 2021
Structure of the Aeropyrum Pernix ORC2 protein (ADPNP-ADP complexes)Structure of the Aeropyrum Pernix ORC2 protein (ADPNP-ADP complexes)
Structural highlights
Function[CDC62_AERPE] Involved in regulation of DNA replication (By similarity). Binds DNA.[HAMAP-Rule:MF_01407][1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedArchaea contain one or more proteins with homology to eukaryotic ORC/Cdc6 proteins. Sequence analysis suggests the existence of at least two subfamilies of these proteins, for which we propose the nomenclature ORC1 and ORC2. We have determined crystal structures of the ORC2 protein from the archaeon Aeropyrum pernix in complexes with ADP or a non-hydrolysable ATP analogue, ADPNP. Between two crystal forms, there are three crystallographically independent views of the ADP complex and two of the ADPNP complex. The protein molecules in the three complexes with ADP adopt very different conformations, while the two complexes with ADPNP are the same. These structures indicate that there is considerable conformational flexibility in ORC2 but that ATP binding stabilises a single conformation. We show that the ORC2 protein can bind DNA, and that this activity is associated with the C-terminal domain of the protein. We present a model for the interaction of the winged helix (WH) domain of ORC2 with DNA that differs from that proposed previously for Pyrobaculum aerophilum ORC/Cdc6. Conformational changes induced by nucleotide binding in Cdc6/ORC from Aeropyrum pernix.,Singleton MR, Morales R, Grainge I, Cook N, Isupov MN, Wigley DB J Mol Biol. 2004 Oct 22;343(3):547-57. PMID:15465044[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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