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1DP8

CRYSTAL STRUCTURE OF THE NITRIC OXIDE BOUND FIXL HEME DOMAIN

Summary for 1DP8
Entry DOI10.2210/pdb1dp8/pdb
Related1BV5 1BV6 1DP6
DescriptorFIXL PROTEIN, NITRIC OXIDE, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
Functional Keywordsheme, fixl heme domain liganded structures, histidine kinase, signal transduction, two component system, oxygen storage-transport complex, oxygen storage/transport
Biological sourceBradyrhizobium japonicum
Total number of polymer chains1
Total formula weight15566.35
Authors
Gong, W.,Hao, B.,Chan, M.K. (deposition date: 1999-12-24, release date: 2000-12-24, Last modification date: 2024-02-07)
Primary citationGong, W.,Hao, B.,Chan, M.K.
New mechanistic insights from structural studies of the oxygen-sensing domain of Bradyrhizobium japonicum FixL.
Biochemistry, 39:3955-3962, 2000
Cited by
PubMed Abstract: 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.
PubMed: 10747783
DOI: 10.1021/bi992346w
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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數據於2024-11-06公開中

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