2eb7: Difference between revisions

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==Overview==

The emergence of bacterial resistance to multiple drugs poses a serious, and growing health concern. Understanding and deciphering the mechanisms, of these multiple drug resistance regulatory proteins through structural, or biochemical means is an important endeavor. Here, we present the, crystal structure of ST1710 from Sulfolobus tokodaii strain 7 in two, different crystal forms, at 1.80 and 2.0A, respectively. The overall, structure of the ST1710 dimer shares the topology of the MarR family of, proteins, with each subunit containing a winged helix-turn-helix, DNA-binding motif. We also show the protein-DNA interactions by, biochemical methods. Our molecular modeling analysis suggested that Asp88, and Arg90 are the key residues in ST1710 involved in the protein-DNA, interactions.

The emergence of bacterial resistance to multiple drugs poses a serious and growing health concern. Understanding and deciphering the mechanisms of these multiple drug resistance regulatory proteins through structural or biochemical means is an important endeavor. Here, we present the crystal structure of ST1710 from Sulfolobus tokodaii strain 7 in two different crystal forms, at 1.80 and 2.0A, respectively. The overall structure of the ST1710 dimer shares the topology of the MarR family of proteins, with each subunit containing a winged helix-turn-helix DNA-binding motif. We also show the protein-DNA interactions by biochemical methods. Our molecular modeling analysis suggested that Asp88 and Arg90 are the key residues in ST1710 involved in the protein-DNA interactions.

==About this Structure==

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==Reference==

Crystal structure of the MarR family regulatory protein, ST1710, from Sulfolobus tokodaii strain 7., Kumarevel T, Tanaka T, Nishio M, Gopinath SC, Takio K, Shinkai A, Kumar PK, Yokoyama S, J Struct Biol. 2007 Sep 8;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17933554 17933554]

Crystal structure of the MarR family regulatory protein, ST1710, from Sulfolobus tokodaii strain 7., Kumarevel T, Tanaka T, Nishio M, Gopinath SC, Takio K, Shinkai A, Kumar PK, Yokoyama S, J Struct Biol. 2008 Jan;161(1):9-17. Epub 2007 Sep 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17933554 17933554]

[[Category: Single protein]]

[[Category: Sulfolobus tokodaii]]

[[Category: Kumarevel, T.S.]]

[[Category: Kumarevel, T S.]]

[[Category: Nishio, M.]]

[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]

[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]

[[Category: Shinkai, A.]]

[[Category: Yokoyama, S.]]

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[[Category: transcription regulator]]

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@@ Line 4: / Line 4: @@
 ==Overview==
-The emergence of bacterial resistance to multiple drugs poses a serious, and growing health concern. Understanding and deciphering the mechanisms, of these multiple drug resistance regulatory proteins through structural, or biochemical means is an important endeavor. Here, we present the, crystal structure of ST1710 from Sulfolobus tokodaii strain 7 in two, different crystal forms, at 1.80 and 2.0A, respectively. The overall, structure of the ST1710 dimer shares the topology of the MarR family of, proteins, with each subunit containing a winged helix-turn-helix, DNA-binding motif. We also show the protein-DNA interactions by, biochemical methods. Our molecular modeling analysis suggested that Asp88, and Arg90 are the key residues in ST1710 involved in the protein-DNA, interactions.
+The emergence of bacterial resistance to multiple drugs poses a serious and growing health concern. Understanding and deciphering the mechanisms of these multiple drug resistance regulatory proteins through structural or biochemical means is an important endeavor. Here, we present the crystal structure of ST1710 from Sulfolobus tokodaii strain 7 in two different crystal forms, at 1.80 and 2.0A, respectively. The overall structure of the ST1710 dimer shares the topology of the MarR family of proteins, with each subunit containing a winged helix-turn-helix DNA-binding motif. We also show the protein-DNA interactions by biochemical methods. Our molecular modeling analysis suggested that Asp88 and Arg90 are the key residues in ST1710 involved in the protein-DNA interactions.
 ==About this Structure==
@@ Line 10: / Line 10: @@
 ==Reference==
-Crystal structure of the MarR family regulatory protein, ST1710, from Sulfolobus tokodaii strain 7., Kumarevel T, Tanaka T, Nishio M, Gopinath SC, Takio K, Shinkai A, Kumar PK, Yokoyama S, J Struct Biol. 2007 Sep 8;. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17933554 17933554]
+Crystal structure of the MarR family regulatory protein, ST1710, from Sulfolobus tokodaii strain 7., Kumarevel T, Tanaka T, Nishio M, Gopinath SC, Takio K, Shinkai A, Kumar PK, Yokoyama S, J Struct Biol. 2008 Jan;161(1):9-17. Epub 2007 Sep 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17933554 17933554]
 [[Category: Single protein]]
 [[Category: Sulfolobus tokodaii]]
-[[Category: Kumarevel, T.S.]]
+[[Category: Kumarevel, T S.]]
 [[Category: Nishio, M.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Shinkai, A.]]
 [[Category: Yokoyama, S.]]
@@ Line 28: / Line 28: @@
 [[Category: transcription regulator]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:12:32 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:08:10 2008''