1fnn

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(New page: 200px<br /><applet load="1fnn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fnn, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[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==
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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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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==
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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].
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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]]
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[[Category: Berger, J.M.]]
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[[Category: Berger, J M.]]
[[Category: DeAngelis, K.]]
[[Category: DeAngelis, K.]]
[[Category: DeRyckere, D.]]
[[Category: DeRyckere, D.]]
[[Category: Liu, J.]]
[[Category: Liu, J.]]
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[[Category: Martin, G.S.]]
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[[Category: Martin, G S.]]
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[[Category: Smith, C.L.]]
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[[Category: Smith, C L.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: orc1]]
[[Category: orc1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:07:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:40:36 2008''

Revision as of 10:40, 21 February 2008


1fnn, resolution 2.0Å

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CRYSTAL STRUCTURE OF CDC6P FROM PYROBACULUM AEROPHILUM

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.

About this Structure

1FNN is a Single protein structure of sequence from Pyrobaculum aerophilum with and as ligands. Full crystallographic information is available from OCA.

Reference

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

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