1fnn

<StructureSection load='1fnn' size='340' side='right' caption='[[1fnn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1fnn]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FNN 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=MG:MAGNESIUM+ION'>MG</scene></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fnn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fnn RCSB], [http://www.ebi.ac.uk/pdbsum/1fnn PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/Q8ZYK1_PYRAE Q8ZYK1_PYRAE]] Involved in regulation of DNA replication (By similarity).[HAMAP-Rule:MF_01407]

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fn/1fnn_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Berger, J M]]

[[Category: DeAngelis, K]]

[[Category: DeRyckere, D]]

[[Category: Liu, J]]

[[Category: Martin, G S]]

[[Category: Smith, C L]]

[[Category: Orc1]]