1hkq
From Proteopedia
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| - | [[Image:1hkq.gif|left|200px]] | + | [[Image:1hkq.gif|left|200px]] |
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| - | '''PPS10 PLASMID DNA REPLICATION INITIATOR PROTEIN REPA. REPLICATION INACTIVE, DIMERIC N-TERMINAL DOMAIN.''' | + | {{Structure |
| + | |PDB= 1hkq |SIZE=350|CAPTION= <scene name='initialview01'>1hkq</scene>, resolution 2.75Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Hg+Binding+Site+For+Chain+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=BEZ:BENZOIC ACID'>BEZ</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''PPS10 PLASMID DNA REPLICATION INITIATOR PROTEIN REPA. REPLICATION INACTIVE, DIMERIC N-TERMINAL DOMAIN.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HKQ is a [ | + | 1HKQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_savastanoi Pseudomonas savastanoi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HKQ OCA]. |
==Reference== | ==Reference== | ||
| - | A conformational switch between transcriptional repression and replication initiation in the RepA dimerization domain., Giraldo R, Fernandez-Tornero C, Evans PR, Diaz-Orejas R, Romero A, Nat Struct Biol. 2003 Jul;10(7):565-71. PMID:[http:// | + | A conformational switch between transcriptional repression and replication initiation in the RepA dimerization domain., Giraldo R, Fernandez-Tornero C, Evans PR, Diaz-Orejas R, Romero A, Nat Struct Biol. 2003 Jul;10(7):565-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12766757 12766757] |
[[Category: Pseudomonas savastanoi]] | [[Category: Pseudomonas savastanoi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: winged-helix]] | [[Category: winged-helix]] | ||
| - | ''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 11:38:21 2008'' |
Revision as of 09:38, 20 March 2008
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| , resolution 2.75Å | |||||||
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| Sites: | |||||||
| Ligands: | , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PPS10 PLASMID DNA REPLICATION INITIATOR PROTEIN REPA. REPLICATION INACTIVE, DIMERIC N-TERMINAL DOMAIN.
Overview
Plasmids are natural vectors for gene transfer. In Gram-negative bacteria, plasmid DNA replication is triggered when monomers of an initiator protein (Rep) bind to direct repeats at the origin sequence. Rep dimers, which are inactive as initiators, bind to an inverse repeat operator, repressing transcription of the rep gene. Rep proteins are composed of N-terminal dimerization and C-terminal DNA-binding domains. Activation of Rep is coupled to dimer dissociation, converting the dimerization domain into a second origin-binding module. Although the structure of the monomeric F plasmid initiator (mRepE) has been determined, the molecular nature of Rep activation remains unknown. Here we report the crystal structure of the dimeric N-terminal domain of the pPS10 plasmid initiator (dRepA). dRepA has a winged-helix fold, as does its homologous domain in mRepE. However, dimerization transforms an interdomain loop and beta-strand (monomeric RepE) into an alpha-helix (dimeric RepA). dRepA resemble the C terminus of eukaryotic and archaeal Cdc6, giving clues to the phylogeny of DNA replication initiators.
About this Structure
1HKQ is a Single protein structure of sequence from Pseudomonas savastanoi. Full crystallographic information is available from OCA.
Reference
A conformational switch between transcriptional repression and replication initiation in the RepA dimerization domain., Giraldo R, Fernandez-Tornero C, Evans PR, Diaz-Orejas R, Romero A, Nat Struct Biol. 2003 Jul;10(7):565-71. PMID:12766757
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