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1b1b
(Difference between revisions)
Categories: Mycobacterium tuberculosis | Single protein | Hol, W G. | Holmes, R K. | Pohl, E. | SO4 | ZN | Ider | Iron depedent regulator | Metal binding protein
(New page: 200px<br /><applet load="1b1b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b1b, resolution 2.60Å" /> '''IRON DEPENDENT REGUL...) |
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| - | [[Image:1b1b.gif|left|200px]]<br /><applet load="1b1b" size=" | + | [[Image:1b1b.gif|left|200px]]<br /><applet load="1b1b" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1b1b, resolution 2.60Å" /> | caption="1b1b, resolution 2.60Å" /> | ||
'''IRON DEPENDENT REGULATOR'''<br /> | '''IRON DEPENDENT REGULATOR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Iron-dependent regulators are a family of metal-activated DNA binding | + | Iron-dependent regulators are a family of metal-activated DNA binding proteins found in several Gram-positive bacteria. These proteins are negative regulators of virulence factors and of proteins of bacterial iron-uptake systems. In this study we present the crystal structure of the iron-dependent regulator (IdeR) from Mycobacterium tuberculosis, the causative agent of tuberculosis. The protein crystallizes in the hexagonal space group P62 with unit cell dimensions a=b=92.6 A, c=63.2 A. The current model comprises the N-terminal DNA-binding domain (residues 1-73) and the dimerization domain (residues 74-140), while the third domain (residues 141-230) is too disordered to be included. The molecule lies on a crystallographic 2-fold axis that generates the functional dimer. The overall structure of the monomer shares many features with the homologous regulator, diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae. The IdeR structure in complex with Zinc reported here is, however, the first wild-type repressor structure with both metal binding sites fully occupied. This crystal structure reveals that both Met10 and most probably the Sgamma of Cys102 are ligands of the second metal binding site. In addition, there are important changes in the tertiary structure between apo-DtxR and holo-IdeR bringing the putative DNA binding helices closer together in the holo repressor. The mechanism by which metal binding may cause these structural changes between apo and holo wild-type repressor is discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 1B1B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with ZN and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1B1B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B1B OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hol, W | + | [[Category: Hol, W G.]] |
| - | [[Category: Holmes, R | + | [[Category: Holmes, R K.]] |
[[Category: Pohl, E.]] | [[Category: Pohl, E.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: mycobacterium tuberculosis]] | [[Category: mycobacterium tuberculosis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:50:28 2008'' |
Revision as of 09:50, 21 February 2008
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IRON DEPENDENT REGULATOR
Overview
Iron-dependent regulators are a family of metal-activated DNA binding proteins found in several Gram-positive bacteria. These proteins are negative regulators of virulence factors and of proteins of bacterial iron-uptake systems. In this study we present the crystal structure of the iron-dependent regulator (IdeR) from Mycobacterium tuberculosis, the causative agent of tuberculosis. The protein crystallizes in the hexagonal space group P62 with unit cell dimensions a=b=92.6 A, c=63.2 A. The current model comprises the N-terminal DNA-binding domain (residues 1-73) and the dimerization domain (residues 74-140), while the third domain (residues 141-230) is too disordered to be included. The molecule lies on a crystallographic 2-fold axis that generates the functional dimer. The overall structure of the monomer shares many features with the homologous regulator, diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae. The IdeR structure in complex with Zinc reported here is, however, the first wild-type repressor structure with both metal binding sites fully occupied. This crystal structure reveals that both Met10 and most probably the Sgamma of Cys102 are ligands of the second metal binding site. In addition, there are important changes in the tertiary structure between apo-DtxR and holo-IdeR bringing the putative DNA binding helices closer together in the holo repressor. The mechanism by which metal binding may cause these structural changes between apo and holo wild-type repressor is discussed.
About this Structure
1B1B is a Single protein structure of sequence from Mycobacterium tuberculosis with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the iron-dependent regulator (IdeR) from Mycobacterium tuberculosis shows both metal binding sites fully occupied., Pohl E, Holmes RK, Hol WG, J Mol Biol. 1999 Jan 22;285(3):1145-56. PMID:9887269
Page seeded by OCA on Thu Feb 21 11:50:28 2008