1dp6
From Proteopedia
(New page: 200px<br /><applet load="1dp6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dp6, resolution 2.3Å" /> '''OXYGEN-BINDING COMPLE...) |
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| - | [[Image:1dp6.gif|left|200px]]<br /><applet load="1dp6" size=" | + | [[Image:1dp6.gif|left|200px]]<br /><applet load="1dp6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1dp6, resolution 2.3Å" /> | caption="1dp6, resolution 2.3Å" /> | ||
'''OXYGEN-BINDING COMPLEX OF FIXL HEME DOMAIN'''<br /> | '''OXYGEN-BINDING COMPLEX OF FIXL HEME DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The FixL heme domain serves as the dioxygen switch in the FixL/FixJ | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1DP6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum] with OXY and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1DP6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bradyrhizobium_japonicum Bradyrhizobium japonicum] with <scene name='pdbligand=OXY:'>OXY</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DP6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bradyrhizobium japonicum]] | [[Category: Bradyrhizobium japonicum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chan, M | + | [[Category: Chan, M K.]] |
[[Category: Gong, W.]] | [[Category: Gong, W.]] | ||
[[Category: Hao, B.]] | [[Category: Hao, B.]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:02 2008'' |
Revision as of 10:19, 21 February 2008
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OXYGEN-BINDING COMPLEX OF FIXL HEME DOMAIN
Overview
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.
About this Structure
1DP6 is a Single protein structure of sequence from Bradyrhizobium japonicum with and as ligands. Full crystallographic information is available from OCA.
Reference
New mechanistic insights from structural studies of the oxygen-sensing domain of Bradyrhizobium japonicum FixL., Gong W, Hao B, Chan MK, Biochemistry. 2000 Apr 11;39(14):3955-62. PMID:10747783
Page seeded by OCA on Thu Feb 21 12:19:02 2008
Categories: Bradyrhizobium japonicum | Single protein | Chan, M K. | Gong, W. | Hao, B. | HEM | OXY | Fixl | Heme | Histidine kinase | Pas domain | Signal transduction
