2z4r
From Proteopedia
(New page: 200px<br /><applet load="2z4r" size="350" color="white" frame="true" align="right" spinBox="true" caption="2z4r, resolution 3.05Å" /> '''Crystal structure of...) |
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| - | [[Image:2z4r.jpg|left|200px]] | + | [[Image:2z4r.jpg|left|200px]] |
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| - | '''Crystal structure of domain III from the Thermotoga maritima replication initiation protein DnaA''' | + | {{Structure |
| + | |PDB= 2z4r |SIZE=350|CAPTION= <scene name='initialview01'>2z4r</scene>, resolution 3.05Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+500'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+B+501'>AC2</scene>, <scene name='pdbsite=AC3:Mg+Binding+Site+For+Residue+C+502'>AC3</scene>, <scene name='pdbsite=AC4:Adp+Binding+Site+For+Residue+A+501'>AC4</scene>, <scene name='pdbsite=AC5:Adp+Binding+Site+For+Residue+B+502'>AC5</scene> and <scene name='pdbsite=AC6:Adp+Binding+Site+For+Residue+C+503'>AC6</scene> | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=ADP:ADENOSINE-5'-DIPHOSPHATE'>ADP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= dnaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of domain III from the Thermotoga maritima replication initiation protein DnaA''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2Z4R is a [ | + | 2Z4R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z4R OCA]. |
==Reference== | ==Reference== | ||
| - | A common mechanism for the ATP-DnaA-dependent formation of open complexes at the replication origin., Ozaki S, Kawakami H, Nakamura K, Fujikawa N, Kagawa W, Park SY, Yokoyama S, Kurumizaka H, Katayama T, J Biol Chem. 2008 Jan 23;. PMID:[http:// | + | A common mechanism for the ATP-DnaA-dependent formation of open complexes at the replication origin., Ozaki S, Kawakami H, Nakamura K, Fujikawa N, Kagawa W, Park SY, Yokoyama S, Kurumizaka H, Katayama T, J Biol Chem. 2008 Jan 23;. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18216012 18216012] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
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[[Category: dna-binding]] | [[Category: dna-binding]] | ||
[[Category: domain iii (atpase domain)]] | [[Category: domain iii (atpase domain)]] | ||
| - | [[Category: national project on protein structural and functional | + | [[Category: national project on protein structural and functional analyse]] |
[[Category: nppsfa]] | [[Category: nppsfa]] | ||
[[Category: nucleotide-binding]] | [[Category: nucleotide-binding]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:52:09 2008'' |
Revision as of 16:52, 20 March 2008
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| , resolution 3.05Å | |||||||
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| Sites: | , , , , and | ||||||
| Ligands: | and | ||||||
| Gene: | dnaA (Thermotoga maritima) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of domain III from the Thermotoga maritima replication initiation protein DnaA
Overview
Initiation of chromosomal replication and its cell cycle-coordinated regulation bear crucial and fundamental mechanisms in most cellular organisms. Escherichia coli DnaA protein forms a homomultimeric complex with the replication origin (oriC). ATP-DnaA multimers unwind the duplex within the oriC unwinding element (DUE). In this study, structural analyses suggested that several residues exposing in the central pore of the putative structure of DnaA multimers could be important for unwinding. Using mutation analyses, we found that, of these candidate residues, DnaA Val-211 and Arg-245 are prerequisite for initiation in vivo and in vitro. Whereas DnaA V211A and R245A proteins retained normal affinities for ATP/ADP and DNA and activity for the ATP-specific conformational change of the initiation complex in vitro, oriC complexes of these mutant proteins were inactive in DUE unwinding and in binding to the single-stranded DUE. Unlike oriC complexes including ADP-DnaA or the mutant DnaA, ATP-DnaA-oriC complexes specifically bound the upper-strand of single-stranded DUE. Specific T-rich sequences within the strand were required for binding. The corresponding conserved residues of the DnaA ortholog in Thermotoga maritima, a most ancient eubacterium, were also required for DUE unwinding, consistent with the idea that the mechanism and regulation for DUE unwinding can be evolutionarily conserved. These findings provide novel insights in mechanisms for the initiation complex's pore-mediated origin unwinding, its ATP/ADP-dependent regulation and helicase loading.
About this Structure
2Z4R is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.
Reference
A common mechanism for the ATP-DnaA-dependent formation of open complexes at the replication origin., Ozaki S, Kawakami H, Nakamura K, Fujikawa N, Kagawa W, Park SY, Yokoyama S, Kurumizaka H, Katayama T, J Biol Chem. 2008 Jan 23;. PMID:18216012
Page seeded by OCA on Thu Mar 20 18:52:09 2008
Categories: Single protein | Thermotoga maritima | Fujikawa, N. | Kagawa, W. | Katayama, T. | Kurumizaka, H. | Ozaki, S. | Park, S Y. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Yokoyama, S. | ADP | MG | Aaa+ atpase | Atp-binding | Cytoplasm | Dna binding protein | Dna replication | Dna-binding | Domain iii (atpase domain) | National project on protein structural and functional analyse | Nppsfa | Nucleotide-binding | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
