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| {{STRUCTURE_1dp9| PDB=1dp9 | SCENE= }} | | {{STRUCTURE_1dp9| PDB=1dp9 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF IMIDAZOLE-BOUND FIXL HEME DOMAIN'''
| | ===CRYSTAL STRUCTURE OF IMIDAZOLE-BOUND FIXL HEME DOMAIN=== |
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| ==Overview==
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| The FixL heme domain serves as the dioxygen switch in the FixL/FixJ two-component system of Rhizobia. Recent structural studies of the Bradyrhizobium japonicum FixL heme domain (BjFixLH) have suggested an allosteric mechanism that is distinct from the classical hemoglobin model. To gain further insight into the FixL sensing mechanism, structures of BjFixLH bound to dioxygen, imidazole, and nitric oxide have been determined. These structures, particularly the structure of BjFixLH bound to its physiological ligand, dioxygen, have helped to address a number of important issues relevant to the BjFixLH sensing mechanism. On the basis of the oxy-BjFixLH structure, a conserved arginine is found to stabilize the dioxygen ligand in a mode reminiscent of the distal histidine in classical myoglobins and hemoglobins. The structure of BjFixLH bound to imidazole elucidates the structural requirements for accommodating sterically bulky ligands. Finally, the structure of BjFixLH bound to nitric oxide provides evidence for a structural intermediate in the heme-driven conformational change. | | The line below this paragraph, {{ABSTRACT_PUBMED_10747783}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10747783 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10747783}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Pas domain family]] | | [[Category: Pas domain family]] |
| [[Category: Two component system]] | | [[Category: Two component system]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:06:42 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:24:42 2008'' |
