2g88: Difference between revisions
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[[Image:2g88.gif|left|200px]] | [[Image:2g88.gif|left|200px]] | ||
'''MSRECA-dATP COMPLEX''' | {{Structure | ||
|PDB= 2g88 |SIZE=350|CAPTION= <scene name='initialview01'>2g88</scene>, resolution 3.20Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=DTP:2'-DEOXYADENOSINE+5'-TRIPHOSPHATE'>DTP</scene> and <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene> | |||
|ACTIVITY= | |||
|GENE= recA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1772 Mycobacterium smegmatis]) | |||
}} | |||
'''MSRECA-dATP COMPLEX''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2G88 is a [ | 2G88 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_smegmatis Mycobacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G88 OCA]. | ||
==Reference== | ==Reference== | ||
Crystallographic identification of an ordered C-terminal domain and a second nucleotide-binding site in RecA: new insights into allostery., Krishna R, Manjunath GP, Kumar P, Surolia A, Chandra NR, Muniyappa K, Vijayan M, Nucleic Acids Res. 2006 Apr 28;34(8):2186-95. Print 2006. PMID:[http:// | Crystallographic identification of an ordered C-terminal domain and a second nucleotide-binding site in RecA: new insights into allostery., Krishna R, Manjunath GP, Kumar P, Surolia A, Chandra NR, Muniyappa K, Vijayan M, Nucleic Acids Res. 2006 Apr 28;34(8):2186-95. Print 2006. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16648362 16648362] | ||
[[Category: Mycobacterium smegmatis]] | [[Category: Mycobacterium smegmatis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: recombination]] | [[Category: recombination]] | ||
''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 17:01:35 2008'' | ||
Revision as of 18:01, 20 March 2008
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| , resolution 3.20Å | |||||||
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| Ligands: | , and | ||||||
| Gene: | recA (Mycobacterium smegmatis) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MSRECA-dATP COMPLEX
OverviewOverview
RecA protein is a crucial and central component of the homologous recombination and DNA repair machinery. Despite numerous studies on the protein, several issues concerning its action, including the allosteric regulation mechanism have remained unclear. Here we report, for the first time, a crystal structure of a complex of Mycobacterium smegmatis RecA (MsRecA) with dATP, which exhibits a fully ordered C-terminal domain, with a second dATP molecule bound to it. ATP binding is an essential step for all activities of RecA, since it triggers the formation of active nucleoprotein filaments. In the crystal filament, dATP at the first site communicates with a dATP of the second site of an adjacent subunit, through conserved residues, suggesting a new route for allosteric regulation. In addition, subtle but definite changes observed in the orientation of the nucleotide at the first site and in the positions of the segment preceding loop L2 as well as in the segment 102-105 situated between the 2 nt, all appear to be concerted and suggestive of a biological role for the second bound nucleotide.
About this StructureAbout this Structure
2G88 is a Single protein structure of sequence from Mycobacterium smegmatis. Full crystallographic information is available from OCA.
ReferenceReference
Crystallographic identification of an ordered C-terminal domain and a second nucleotide-binding site in RecA: new insights into allostery., Krishna R, Manjunath GP, Kumar P, Surolia A, Chandra NR, Muniyappa K, Vijayan M, Nucleic Acids Res. 2006 Apr 28;34(8):2186-95. Print 2006. PMID:16648362
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