1lsv

<table><tr><td colspan='2'>[[1lsv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhizobacterium_japonicum"_kirchner_1896 "rhizobacterium japonicum" kirchner 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1LSV FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1dp6|1dp6]], [[1dp8|1dp8]], [[1dp9|1dp9]], [[1drm|1drm]], [[1lsw|1lsw]], [[1lsx|1lsx]], [[1lt0|1lt0]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FixL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=375 "Rhizobacterium japonicum" Kirchner 1896])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1lsv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lsv OCA], [http://pdbe.org/1lsv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lsv RCSB], [http://www.ebi.ac.uk/pdbsum/1lsv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lsv ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/FIXL_BRAJA FIXL_BRAJA]] Putative oxygen sensor; modulates the activity of FixJ, a transcriptional activator of nitrogen fixation fixK gene. FixL probably acts as a kinase that phosphorylates FixJ.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:12390021</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1lsv" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Rhizobacterium japonicum kirchner 1896]]

[[Category: Arndt, J]]

[[Category: Chan, M K]]

[[Category: Hao, B]]

[[Category: Isaza, C]]

[[Category: Soltis, M]]

[[Category: Transferase]]