1fnn
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1fnn |SIZE=350|CAPTION= <scene name='initialview01'>1fnn</scene>, resolution 2.0Å | |PDB= 1fnn |SIZE=350|CAPTION= <scene name='initialview01'>1fnn</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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.ebi.ac.uk/pdbsum/1fnn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fnn RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Martin, G S.]] | [[Category: Martin, G S.]] | ||
[[Category: Smith, C L.]] | [[Category: Smith, C L.]] | ||
| - | [[Category: ADP]] | ||
| - | [[Category: MG]] | ||
[[Category: aaa protein]] | [[Category: aaa protein]] | ||
[[Category: cdc18]] | [[Category: cdc18]] | ||
| Line 37: | Line 38: | ||
[[Category: orc1]] | [[Category: orc1]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:26:30 2008'' |
Revision as of 17:26, 30 March 2008
| |||||||
| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Sun Mar 30 20:26:30 2008
