1ghh: Difference between revisions
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[[Image:1ghh.gif|left|200px]] | [[Image:1ghh.gif|left|200px]] | ||
'''SOLUTION STRUCTURE OF DINI''' | {{Structure | ||
|PDB= 1ghh |SIZE=350|CAPTION= <scene name='initialview01'>1ghh</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''SOLUTION STRUCTURE OF DINI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1GHH is a [ | 1GHH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 1F0A. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GHH OCA]. | ||
==Reference== | ==Reference== | ||
Solution structure of DinI provides insight into its mode of RecA inactivation., Ramirez BE, Voloshin ON, Camerini-Otero RD, Bax A, Protein Sci. 2000 Nov;9(11):2161-9. PMID:[http:// | Solution structure of DinI provides insight into its mode of RecA inactivation., Ramirez BE, Voloshin ON, Camerini-Otero RD, Bax A, Protein Sci. 2000 Nov;9(11):2161-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11152126 11152126] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: reca]] | [[Category: reca]] | ||
''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 11:23:07 2008'' | ||
Revision as of 12:23, 20 March 2008
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SOLUTION STRUCTURE OF DINI
OverviewOverview
The Escherichia coli RecA protein triggers both DNA repair and mutagenesis in a process known as the SOS response. The 81-residue E. coli protein DinI inhibits activity of RecA in vivo. The solution structure of DinI has been determined by multidimensional triple resonance NMR spectroscopy, using restraints derived from two sets of residual dipolar couplings, obtained in bicelle and phage media, supplemented with J couplings and a moderate number of NOE restraints. DinI has an alpha/beta fold comprised of a three-stranded beta-sheet and two alpha-helices. The beta-sheet topology is unusual: the central strand is flanked by a parallel and an antiparallel strand and the sheet is remarkably flat. The structure of DinI shows that six negatively charged Glu and Asp residues on DinI's kinked C-terminal alpha-helix form an extended, negatively charged ridge. We propose that this ridge mimics the electrostatic character of the DNA phospodiester backbone, thereby enabling DinI to compete with single-stranded DNA for RecA binding. Biochemical data confirm that DinI is able to displace ssDNA from RecA.
About this StructureAbout this Structure
1GHH is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1F0A. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of DinI provides insight into its mode of RecA inactivation., Ramirez BE, Voloshin ON, Camerini-Otero RD, Bax A, Protein Sci. 2000 Nov;9(11):2161-9. PMID:11152126
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