2fmy
From Proteopedia
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| - | [[Image:2fmy.jpg|left|200px]] | + | [[Image:2fmy.jpg|left|200px]] |
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| - | '''CO-dependent transcription factor CooA from Carboxydothermus hydrogenoformans (Imidazole-bound form)''' | + | {{Structure |
| + | |PDB= 2fmy |SIZE=350|CAPTION= <scene name='initialview01'>2fmy</scene>, resolution 2.20Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> and <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CO-dependent transcription factor CooA from Carboxydothermus hydrogenoformans (Imidazole-bound form)''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2FMY is a [ | + | 2FMY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans Carboxydothermus hydrogenoformans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FMY OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of CO-sensing transcription activator CooA bound to exogenous ligand imidazole., Komori H, Inagaki S, Yoshioka S, Aono S, Higuchi Y, J Mol Biol. 2007 Mar 30;367(3):864-71. Epub 2007 Jan 23. PMID:[http:// | + | Crystal structure of CO-sensing transcription activator CooA bound to exogenous ligand imidazole., Komori H, Inagaki S, Yoshioka S, Aono S, Higuchi Y, J Mol Biol. 2007 Mar 30;367(3):864-71. Epub 2007 Jan 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17292914 17292914] |
[[Category: Carboxydothermus hydrogenoformans]] | [[Category: Carboxydothermus hydrogenoformans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: dna transcription regulator]] | [[Category: dna transcription regulator]] | ||
| - | ''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 16:54:23 2008'' |
Revision as of 14:54, 20 March 2008
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| , resolution 2.20Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CO-dependent transcription factor CooA from Carboxydothermus hydrogenoformans (Imidazole-bound form)
Overview
CooA is a CO-dependent transcriptional activator and transmits a CO-sensing signal to a DNA promoter that controls the expression of the genes responsible for CO metabolism. CooA contains a b-type heme as the active site for sensing CO. CO binding to the heme induces a conformational change that switches CooA from an inactive to an active DNA-binding form. Here, we report the crystal structure of an imidazole-bound form of CooA from Carboxydothermus hydrogenoformans (Ch-CooA). In the resting form, Ch-CooA has a six-coordinate ferrous heme with two endogenous axial ligands, the alpha-amino group of the N-terminal amino acid and a histidine residue. The N-terminal amino group of CooA that is coordinated to the heme iron is replaced by CO. This substitution presumably triggers a structural change leading to the active form. The crystal structure of Ch-CooA reveals that imidazole binds to the heme, which replaces the N terminus, as does CO. The dissociated N terminus is positioned approximately 16 A from the heme iron in the imidazole-bound form. In addition, the heme plane is rotated by 30 degrees about the normal of the porphyrin ring compared to that found in the inactive form of Rhodospirillum rubrum CooA. Even though the ligand exchange, imidazole-bound Ch-CooA remains in the inactive form for DNA binding. These results indicate that the release of the N terminus resulting from imidazole binding is not sufficient to activate CooA. The structure provides new insights into the structural changes required to achieve activation.
About this Structure
2FMY is a Single protein structure of sequence from Carboxydothermus hydrogenoformans. Full crystallographic information is available from OCA.
Reference
Crystal structure of CO-sensing transcription activator CooA bound to exogenous ligand imidazole., Komori H, Inagaki S, Yoshioka S, Aono S, Higuchi Y, J Mol Biol. 2007 Mar 30;367(3):864-71. Epub 2007 Jan 23. PMID:17292914
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