1zs3

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{{STRUCTURE_1zs3| PDB=1zs3 | SCENE= }}
{{STRUCTURE_1zs3| PDB=1zs3 | SCENE= }}
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'''The crystal structure of the Lactococcus lactis MG1363 DpsB protein'''
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===The crystal structure of the Lactococcus lactis MG1363 DpsB protein===
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==Overview==
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Dps proteins play a major role in the protection of bacterial DNA from damage by reactive oxygen species. Previous studies have implicated the extended lysine-containing N-terminal regions of Dps subunits in DNA binding, but this part of the structure has not previously been observed crystallographically. Here the structures of two Dps proteins (DpsA and DpsB) from Lactococcus lactis MG1363 reveal for the first time the presence of an N-terminal alpha helix that extends from the core of the Dps subunit. Consequently, the N-terminal helices are displayed in parallel pairs on the exterior of the dodecameric Dps assemblies. Both DpsA and DpsB bind DNA. Deletion of the DpsA N-terminal helix impaired DNA binding. The N-terminal Lys residues of Escherichia coli Dps have been implicated in DNA binding. Replacement of the lactococcal DpsA Lys residues 9, 15 and 16 by Glu did not inhibit DNA binding. However, DNA binding was inhibited by EDTA, suggesting a role for cations in DNA binding. In contrast to E. coli, Bacillus brevis and Mycobacterium smegmatis Dps:DNA complexes, in which DNA interacts with crystalline Dps phases, L. lactis DNA:Dps complexes appeared as non-crystalline aggregates of protein and DNA in electron micrographs.
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{{ABSTRACT_PUBMED_16091047}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
The crystal structures of Lactococcus lactis MG1363 Dps proteins reveal the presence of an N-terminal helix that is required for DNA binding., Stillman TJ, Upadhyay M, Norte VA, Sedelnikova SE, Carradus M, Tzokov S, Bullough PA, Shearman CA, Gasson MJ, Williams CH, Artymiuk PJ, Green J, Mol Microbiol. 2005 Aug;57(4):1101-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16091047 16091047]
The crystal structures of Lactococcus lactis MG1363 Dps proteins reveal the presence of an N-terminal helix that is required for DNA binding., Stillman TJ, Upadhyay M, Norte VA, Sedelnikova SE, Carradus M, Tzokov S, Bullough PA, Shearman CA, Gasson MJ, Williams CH, Artymiuk PJ, Green J, Mol Microbiol. 2005 Aug;57(4):1101-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16091047 16091047]
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Two operons that encode FNR-like proteins in Lactococcus lactis., Gostick DO, Griffin HG, Shearman CA, Scott C, Green J, Gasson MJ, Guest JR, Mol Microbiol. 1999 Mar;31(5):1523-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10200970 10200970]
[[Category: Artymiuk, P J.]]
[[Category: Artymiuk, P J.]]
[[Category: Bullough, P A.]]
[[Category: Bullough, P A.]]
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[[Category: Lactic acid bacteria]]
[[Category: Lactic acid bacteria]]
[[Category: Oxidative stress]]
[[Category: Oxidative stress]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:00:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:45:29 2008''

Revision as of 13:45, 28 July 2008

Image:1zs3.png

Template:STRUCTURE 1zs3

The crystal structure of the Lactococcus lactis MG1363 DpsB protein

Template:ABSTRACT PUBMED 16091047

About this Structure

Full crystallographic information is available from OCA.

Reference

The crystal structures of Lactococcus lactis MG1363 Dps proteins reveal the presence of an N-terminal helix that is required for DNA binding., Stillman TJ, Upadhyay M, Norte VA, Sedelnikova SE, Carradus M, Tzokov S, Bullough PA, Shearman CA, Gasson MJ, Williams CH, Artymiuk PJ, Green J, Mol Microbiol. 2005 Aug;57(4):1101-12. PMID:16091047

Two operons that encode FNR-like proteins in Lactococcus lactis., Gostick DO, Griffin HG, Shearman CA, Scott C, Green J, Gasson MJ, Guest JR, Mol Microbiol. 1999 Mar;31(5):1523-35. PMID:10200970

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