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| | <StructureSection load='4b2k' size='340' side='right'caption='[[4b2k]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='4b2k' size='340' side='right'caption='[[4b2k]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4b2k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hals3 Hals3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B2K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4b2k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halobacterium_salinarum_R1 Halobacterium salinarum R1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B2K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RBF:RIBOFLAVIN'>RBF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=4IN:4-AMINO-L-TRYPTOPHAN'>4IN</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4IN:4-AMINO-L-TRYPTOPHAN'>4IN</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RBF:RIBOFLAVIN'>RBF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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;'>[[2cc8|2cc8]], [[2ccb|2ccb]], [[2vx9|2vx9]], [[4b2h|4b2h]], [[4b2j|4b2j]], [[4b2m|4b2m]]</div></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=4b2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b2k OCA], [https://pdbe.org/4b2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b2k RCSB], [https://www.ebi.ac.uk/pdbsum/4b2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b2k 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=4b2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b2k OCA], [https://pdbe.org/4b2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b2k RCSB], [https://www.ebi.ac.uk/pdbsum/4b2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b2k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/DODEC_HALS3 DODEC_HALS3]] May function as storage protein that sequesters riboflavin and related compounds, thereby protecting the cell against undesirable reactions mediated by the free flavins. Binds and sequesters riboflavin, lumiflavin and lumichrome. Can also bind FAD and FMN (in vitro), but has low affinity for FAD and even lower affinity for FMN. Protects bound flavins against light damage; Trp-36 rapidly quenches the flavin excited state. Promotes the conversion of bound riboflavin to lumichrome.<ref>PMID:12679016</ref> <ref>PMID:16460756</ref> <ref>PMID:17027852</ref> <ref>PMID:19224924</ref> <ref>PMID:20408700</ref>
| + | [https://www.uniprot.org/uniprot/DODEC_HALS3 DODEC_HALS3] May function as storage protein that sequesters riboflavin and related compounds, thereby protecting the cell against undesirable reactions mediated by the free flavins. Binds and sequesters riboflavin, lumiflavin and lumichrome. Can also bind FAD and FMN (in vitro), but has low affinity for FAD and even lower affinity for FMN. Protects bound flavins against light damage; Trp-36 rapidly quenches the flavin excited state. Promotes the conversion of bound riboflavin to lumichrome.<ref>PMID:12679016</ref> <ref>PMID:16460756</ref> <ref>PMID:17027852</ref> <ref>PMID:19224924</ref> <ref>PMID:20408700</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Hals3]] | + | [[Category: Halobacterium salinarum R1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Budisa, N]] | + | [[Category: Budisa N]] |
| - | [[Category: Dreuw, A]] | + | [[Category: Dreuw A]] |
| - | [[Category: Grininger, M]] | + | [[Category: Grininger M]] |
| - | [[Category: Hoesl, M]] | + | [[Category: Hoesl M]] |
| - | [[Category: Oesterhelt, D]] | + | [[Category: Oesterhelt D]] |
| - | [[Category: Serdjukow, S]] | + | [[Category: Serdjukow S]] |
| - | [[Category: Staudt, H]] | + | [[Category: Staudt H]] |
| - | [[Category: Wachtveitl, J]] | + | [[Category: Wachtveitl J]] |
| - | [[Category: Flavoprotein]]
| + | |
| - | [[Category: Protein reaction control]]
| + | |
| Structural highlights
4b2k is a 1 chain structure with sequence from Halobacterium salinarum R1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.7Å |
| Ligands: | , , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
DODEC_HALS3 May function as storage protein that sequesters riboflavin and related compounds, thereby protecting the cell against undesirable reactions mediated by the free flavins. Binds and sequesters riboflavin, lumiflavin and lumichrome. Can also bind FAD and FMN (in vitro), but has low affinity for FAD and even lower affinity for FMN. Protects bound flavins against light damage; Trp-36 rapidly quenches the flavin excited state. Promotes the conversion of bound riboflavin to lumichrome.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
Tamed electrons: To manipulate a protein photocycle in a directed manner, the flavoprotein dodecin was endoscopically modified at its key amino acid tryptophan with substituents carefully selected by their structural and electronic influence. The approach is ideal in the precision of rational protein engineering, and allows correlating tryptophan ionization potentials and electron transfer rates in a Marcus model.
Directed Manipulation of a Flavoprotein Photocycle.,Staudt H, Hoesl MG, Dreuw A, Serdjukow S, Oesterhelt D, Budisa N, Wachtveitl J, Grininger M Angew Chem Int Ed Engl. 2013 Jul 1. doi: 10.1002/anie.201302334. PMID:23818044[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bieger B, Essen LO, Oesterhelt D. Crystal structure of halophilic dodecin: a novel, dodecameric flavin binding protein from Halobacterium salinarum. Structure. 2003 Apr;11(4):375-85. PMID:12679016
- ↑ Grininger M, Zeth K, Oesterhelt D. Dodecins: a family of lumichrome binding proteins. J Mol Biol. 2006 Mar 31;357(3):842-57. Epub 2006 Jan 18. PMID:16460756 doi:10.1016/j.jmb.2005.12.072
- ↑ Grininger M, Seiler F, Zeth K, Oesterhelt D. Dodecin sequesters FAD in closed conformation from the aqueous solution. J Mol Biol. 2006 Dec 8;364(4):561-6. Epub 2006 Sep 5. PMID:17027852 doi:10.1016/j.jmb.2006.08.083
- ↑ Grininger M, Staudt H, Johansson P, Wachtveitl J, Oesterhelt D. Dodecin is the key player in flavin homeostasis of archaea. J Biol Chem. 2009 May 8;284(19):13068-76. Epub 2009 Feb 17. PMID:19224924 doi:10.1074/jbc.M808063200
- ↑ Grininger M, Noll G, Trawoger S, Sinner EK, Oesterhelt D. Electrochemical switching of the flavoprotein dodecin at gold surfaces modified by flavin-DNA hybrid linkers. Biointerphases. 2008 Sep;3(3):51-8. PMID:20408700 doi:10.1116/1.2965134
- ↑ Staudt H, Hoesl MG, Dreuw A, Serdjukow S, Oesterhelt D, Budisa N, Wachtveitl J, Grininger M. Directed Manipulation of a Flavoprotein Photocycle. Angew Chem Int Ed Engl. 2013 Jul 1. doi: 10.1002/anie.201302334. PMID:23818044 doi:10.1002/anie.201302334
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