2it0
From Proteopedia
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| - | [[Image:2it0.gif|left|200px]] | + | [[Image:2it0.gif|left|200px]] |
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| - | '''Crystal structure of a two-domain IdeR-DNA complex crystal form II''' | + | {{Structure |
| + | |PDB= 2it0 |SIZE=350|CAPTION= <scene name='initialview01'>2it0</scene>, resolution 2.600Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=ACT:ACETATE ION'>ACT</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= IdeR,dtxR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of a two-domain IdeR-DNA complex crystal form II''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2IT0 is a [ | + | 2IT0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IT0 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structures, metal activation, and DNA-binding properties of two-domain IdeR from Mycobacterium tuberculosis., Wisedchaisri G, Chou CJ, Wu M, Roach C, Rice AE, Holmes RK, Beeson C, Hol WG, Biochemistry. 2007 Jan 16;46(2):436-47. PMID:[http:// | + | Crystal structures, metal activation, and DNA-binding properties of two-domain IdeR from Mycobacterium tuberculosis., Wisedchaisri G, Chou CJ, Wu M, Roach C, Rice AE, Holmes RK, Beeson C, Hol WG, Biochemistry. 2007 Jan 16;46(2):436-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17209554 17209554] |
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dna-binding protein]] | [[Category: dna-binding protein]] | ||
| - | ''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 17:32:56 2008'' |
Revision as of 15:32, 20 March 2008
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| , resolution 2.600Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | IdeR,dtxR (Mycobacterium tuberculosis) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a two-domain IdeR-DNA complex crystal form II
Overview
The iron-dependent regulator IdeR is a key transcriptional regulator of iron uptake in Mycobacterium tuberculosis. In order to increase our insight into the role of the SH3-like third domain of this essential regulator, the metal-binding and DNA-binding properties of two-domain IdeR (2D-IdeR) whose SH3-like domain has been truncated were characterized. The equilibrium dissociation constants for Co2+ and Ni2+ activation of 2D-IdeR for binding to the fxbA operator and the DNA-binding affinities of 2D-IdeR in the presence of excess metal ions were estimated using fluorescence spectroscopy. 2D-IdeR binds to fxbA operator DNA with similar affinity as full-length IdeR in the presence of excess metal ion. However, the Ni2+ concentrations required to activate 2D-IdeR for DNA binding appear to be smaller than that for full-length IdeR while the concentration of Co2+ required for activation remains the same. We have determined the crystal structures of Ni2+-activated 2D-IdeR at 1.96 A resolution and its double dimer complex with the mbtA-mbtB operator DNA in two crystal forms at 2.4 A and 2.6 A, the highest resolutions for DNA complexes for any structures of iron-dependent regulator family members so far. The 2D-IdeR-DNA complex structures confirm the specificity of Ser37 and Pro39 for thymine bases and suggest preferential contacts of Gln43 to cytosine bases of the DNA. In addition, our 2D-IdeR structures reveal a remarkable property of the TEV cleavage sequence remaining after removal of the C-terminal His6. This C-terminal tail promotes crystal contacts by forming a beta-sheet with the corresponding tail of neighboring subunits in two unrelated structures of 2D-IdeR, one with and one without DNA. The contact-promoting properties of this C-terminal TEV cleavage sequence may be beneficial for crystallizing other proteins.
About this Structure
2IT0 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.
Reference
Crystal structures, metal activation, and DNA-binding properties of two-domain IdeR from Mycobacterium tuberculosis., Wisedchaisri G, Chou CJ, Wu M, Roach C, Rice AE, Holmes RK, Beeson C, Hol WG, Biochemistry. 2007 Jan 16;46(2):436-47. PMID:17209554
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