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New page: left|200px<br /><applet load="1fnn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fnn, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1fnn.gif|left|200px]]<br /><applet load="1fnn" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1fnn.gif|left|200px]]<br /><applet load="1fnn" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1fnn, resolution 2.0&Aring;" />
caption="1fnn, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF CDC6P FROM PYROBACULUM AEROPHILUM'''<br />
'''CRYSTAL STRUCTURE OF CDC6P FROM PYROBACULUM AEROPHILUM'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1FNN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FNN OCA].  
1FNN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrobaculum_aerophilum Pyrobaculum aerophilum] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FNN OCA].  


==Reference==
==Reference==
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[[Category: Pyrobaculum aerophilum]]
[[Category: Pyrobaculum aerophilum]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Berger, J.M.]]
[[Category: Berger, J M.]]
[[Category: DeAngelis, K.]]
[[Category: DeAngelis, K.]]
[[Category: DeRyckere, D.]]
[[Category: DeRyckere, D.]]
[[Category: Liu, J.]]
[[Category: Liu, J.]]
[[Category: Martin, G.S.]]
[[Category: Martin, G S.]]
[[Category: Smith, C.L.]]
[[Category: Smith, C L.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: orc1]]
[[Category: orc1]]


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