1lsv
From Proteopedia
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|PDB= 1lsv |SIZE=350|CAPTION= <scene name='initialview01'>1lsv</scene>, resolution 2.40Å | |PDB= 1lsv |SIZE=350|CAPTION= <scene name='initialview01'>1lsv</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= FixL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=375 Bradyrhizobium japonicum]) | |GENE= FixL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=375 Bradyrhizobium japonicum]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1dp6|1DP6]], [[1dp8|1DP8]], [[1dp9|1DP9]], [[1drm|1DRM]], [[1lsw|1LSW]], [[1lsx|1LSX]], [[1lt0|1LT0]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsv OCA], [http://www.ebi.ac.uk/pdbsum/1lsv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lsv RCSB]</span> | ||
}} | }} | ||
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[[Category: Isaza, C.]] | [[Category: Isaza, C.]] | ||
[[Category: Soltis, M.]] | [[Category: Soltis, M.]] | ||
- | [[Category: CMO]] | ||
- | [[Category: HEM]] | ||
[[Category: pas fold]] | [[Category: pas fold]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:06:58 2008'' |
Revision as of 19:07, 30 March 2008
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, resolution 2.40Å | |||||||
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Ligands: | , | ||||||
Gene: | FixL (Bradyrhizobium japonicum) | ||||||
Related: | 1DP6, 1DP8, 1DP9, 1DRM, 1LSW, 1LSX, 1LT0
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of the CO-bound BjFixL heme domain
Overview
Structures of the Bradyrhizobium japonicum FixL heme domain have been determined in the absence and presence of specific ligands to elucidate the detailed features of its O2 sensing mechanism. The putative roles of spin-state and steric hindrance were evaluated by the structure determination of ferrous CO-bound BjFixLH and correlating its features with other ligand-bound structures. As found for NO-BjFixLH, no protein conformational change was observed in CO-BjFixLH, suggesting a more complicated mechanism than solely spin state or ligand sterics. To evaluate the role of oxidation state, the structure of the ferrous deoxy-BjFixLH was determined. The structure of deoxy-BjFixLH was found to be virtually identical to the structure of the ferric met-BjFixLH. The role of hydrogen bonding of substrates to a heme-pocket water was evaluated by determining the structure of BjFixLH bound to 1-methyl-imidazole that cannot form a hydrogen bond with this water. In this case, the heme-mediated conformational change was observed, limiting the potential importance of this interaction. Finally, the structure of cyanomet-BjFixLH was revisited to rule out concerns regarding the partial occupancy of the cyanide ligand in a previous structure. In the revised structure, Arg 220 was found to move into the heme pocket to form a hydrogen bond to the bound cyanide ligand. The implications of these results on FixL's sensing mechanism are discussed.
About this Structure
1LSV is a Single protein structure of sequence from Bradyrhizobium japonicum. Full crystallographic information is available from OCA.
Reference
Structure-based mechanism of O2 sensing and ligand discrimination by the FixL heme domain of Bradyrhizobium japonicum., Hao B, Isaza C, Arndt J, Soltis M, Chan MK, Biochemistry. 2002 Oct 29;41(43):12952-8. PMID:12390021
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