1zs3
From Proteopedia
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| - | [[Image:1zs3.gif|left|200px]] | + | [[Image:1zs3.gif|left|200px]] |
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| - | '''The crystal structure of the Lactococcus lactis MG1363 DpsB protein''' | + | {{Structure |
| + | |PDB= 1zs3 |SIZE=350|CAPTION= <scene name='initialview01'>1zs3</scene>, resolution 2.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= flpB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 Lactococcus lactis]) | ||
| + | }} | ||
| + | |||
| + | '''The crystal structure of the Lactococcus lactis MG1363 DpsB protein''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ZS3 is a [ | + | 1ZS3 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZS3 OCA]. |
==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:// | + | 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] |
[[Category: Lactococcus lactis]] | [[Category: Lactococcus lactis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: Williams, C H.]] | [[Category: Williams, C H.]] | ||
[[Category: dna binding]] | [[Category: dna binding]] | ||
| - | [[Category: | + | [[Category: dp]] |
[[Category: lactic acid bacteria]] | [[Category: lactic acid bacteria]] | ||
[[Category: oxidative stress]] | [[Category: oxidative stress]] | ||
| - | ''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 15:39:11 2008'' |
Revision as of 13:39, 20 March 2008
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| , resolution 2.70Å | |||||||
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| Gene: | flpB (Lactococcus lactis) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structure of the Lactococcus lactis MG1363 DpsB protein
Overview
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.
About this Structure
1ZS3 is a Protein complex structure of sequences from Lactococcus lactis. 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
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