1fnn
From Proteopedia
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<StructureSection load='1fnn' size='340' side='right'caption='[[1fnn]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1fnn' size='340' side='right'caption='[[1fnn]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1fnn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1fnn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FNN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FNN FirstGlance]. <br> |
| - | </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=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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=MG:MAGNESIUM+ION'>MG</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=1fnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fnn OCA], [https://pdbe.org/1fnn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fnn RCSB], [https://www.ebi.ac.uk/pdbsum/1fnn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fnn ProSAT]</span></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=1fnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fnn OCA], [https://pdbe.org/1fnn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fnn RCSB], [https://www.ebi.ac.uk/pdbsum/1fnn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fnn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/Q8ZYK1_PYRAE Q8ZYK1_PYRAE] Involved in regulation of DNA replication (By similarity).[HAMAP-Rule:MF_01407] | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fnn ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fnn ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Cdc6/Cdc18 is a conserved and essential component of prereplication complexes. The 2.0 A crystal structure of an archaeal Cdc6 ortholog, in conjunction with a mutational analysis of the homologous Cdc18 protein from Schizosaccharomyces pombe, reveals novel aspects of Cdc6/Cdc18 function. Two domains of Cdc6 form an AAA+-type nucleotide binding fold that is observed bound to Mg.ADP. A third domain adopts a winged-helix fold similar to known DNA binding modules. Sequence comparisons show that the winged-helix domain is conserved in Orc1, and mutagenesis data demonstrate that this region of Cdc6/Cdc18 is required for function in vivo. Additional mutational analyses suggest that nucleotide binding and/or hydrolysis by Cdc6/Cdc18 is required not only for progression through S phase, but also for maintenance of checkpoint control during S phase. | ||
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| - | Structure and function of Cdc6/Cdc18: implications for origin recognition and checkpoint control.,Liu J, Smith CL, DeRyckere D, DeAngelis K, Martin GS, Berger JM Mol Cell. 2000 Sep;6(3):637-48. PMID:11030343<ref>PMID:11030343</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1fnn" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 51768]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Berger | + | [[Category: Pyrobaculum aerophilum]] |
| - | [[Category: DeAngelis | + | [[Category: Berger JM]] |
| - | [[Category: DeRyckere | + | [[Category: DeAngelis K]] |
| - | [[Category: Liu | + | [[Category: DeRyckere D]] |
| - | [[Category: Martin | + | [[Category: Liu J]] |
| - | [[Category: Smith | + | [[Category: Martin GS]] |
| - | + | [[Category: Smith CL]] | |
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Current revision
CRYSTAL STRUCTURE OF CDC6P FROM PYROBACULUM AEROPHILUM
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