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| | ==Solution structure of Synechococcus sp. PCC 7002 hemoglobin== | | ==Solution structure of Synechococcus sp. PCC 7002 hemoglobin== |
| - | <StructureSection load='2ksc' size='340' side='right'caption='[[2ksc]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''> | + | <StructureSection load='2ksc' size='340' side='right'caption='[[2ksc]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ksc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Agmenellum_quadruplicatum Agmenellum quadruplicatum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KSC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ksc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_sp._PCC_7002 Synechococcus sp. PCC 7002]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KSC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEB:HEME+B/C'>HEB</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 16 models</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glbN, SYNPCC7002_A1621 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32049 Agmenellum quadruplicatum])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ksc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ksc OCA], [https://pdbe.org/2ksc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ksc RCSB], [https://www.ebi.ac.uk/pdbsum/2ksc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ksc ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ksc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ksc OCA], [https://pdbe.org/2ksc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ksc RCSB], [https://www.ebi.ac.uk/pdbsum/2ksc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ksc ProSAT]</span></td></tr> |
| | </table> | | </table> |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ks/2ksc_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ks/2ksc_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Agmenellum quadruplicatum]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Falzone, C J]] | + | [[Category: Synechococcus sp. PCC 7002]] |
| - | [[Category: Lecomte, J T.J]]
| + | [[Category: Falzone CJ]] |
| - | [[Category: Vuletich, D A]] | + | [[Category: Lecomte JTJ]] |
| - | [[Category: 2/2 hemoglobin]] | + | [[Category: Vuletich DA]] |
| - | [[Category: Glbn]] | + | |
| - | [[Category: Hemeprotein]]
| + | |
| - | [[Category: Trhbn]]
| + | |
| - | [[Category: Unknown function]]
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| Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Cyanobacterium Synechococcus sp. PCC 7002 contains a single gene (glbN) coding for GlbN, a protein of the 2/2 hemoglobin lineage. The precise function of GlbN is not known, but comparison to similar 2/2 hemoglobins suggests that reversible dioxygen binding is not its main activity. In this report, the results of in vitro and in vivo experiments probing the role of GlbN are presented. Transcription profiling indicated that glbN is not strongly regulated under any of a large number of growth conditions and that the gene is probably constitutively expressed. High levels of nitrate, used as the sole source of nitrogen, and exposure to nitric oxide were tolerated better by the wild-type strain than a glbN null mutant, whereas overproduction of GlbN in the null mutant background restored the wild-type growth. The cellular contents of reactive oxygen/nitrogen species were elevated in the null mutant under all conditions and were highest under NO challenge or in the presence of high nitrate concentrations. GlbN overproduction attenuated these contents significantly under the latter conditions. The analysis of cell extracts revealed that the heme of GlbN was covalently bound to overproduced GlbN apoprotein in cells grown under microoxic conditions. A peroxidase assay showed that purified GlbN does not possess significant hydrogen peroxidase activity. It was concluded that GlbN protects cells from reactive nitrogen species that could be encountered naturally during growth on nitrate or under denitrifying conditions. The solution structure of covalently modified GlbN was determined and used to rationalize some of its chemical properties.
Functional and structural characterization of the 2/2 hemoglobin from Synechococcus sp. PCC 7002.,Scott NL, Xu Y, Shen G, Vuletich DA, Falzone CJ, Li Z, Ludwig M, Pond MP, Preimesberger MR, Bryant DA, Lecomte JT Biochemistry. 2010 Aug 24;49(33):7000-11. PMID:20669934[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Scott NL, Xu Y, Shen G, Vuletich DA, Falzone CJ, Li Z, Ludwig M, Pond MP, Preimesberger MR, Bryant DA, Lecomte JT. Functional and structural characterization of the 2/2 hemoglobin from Synechococcus sp. PCC 7002. Biochemistry. 2010 Aug 24;49(33):7000-11. PMID:20669934 doi:10.1021/bi100463d
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