2vx9

From Proteopedia

(Difference between revisions)

Revision as of 11:48, 30 March 2022

H. salinarum dodecin E45A mutant

Structural highlights

2vx9 is a 1 chain structure with sequence from Hals3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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]

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

Flavins are employed to transform physical input into biological output signals. In this function, flavins catalyze a variety of light-induced reactions and redox processes. However, nature also provides flavoproteins with the ability to uncouple the mediation of signals. Such proteins are the riboflavin-binding proteins (RfBPs) with their function to store riboflavin for fast delivery of FMN and FAD. Here we present in vitro and in vivo data showing that the recently discovered archaeal dodecin is an RfBP, and we reveal that riboflavin storage is not restricted to eukaryotes. However, the function of the prokaryotic RfBP dodecin seems to be adapted to the requirement of a monocellular organism. While in eukaryotes RfBPs are involved in trafficking riboflavin, and dodecin is responsible for the flavin homeostasis of the cell. Although only 68 amino acids in length, dodecin is of high functional versatility in neutralizing riboflavin to protect the cellular environment from uncontrolled flavin reactivity. Besides the predominant ultrafast quenching of excited states, dodecin prevents light-induced riboflavin reactivity by the selective degradation of riboflavin to lumichrome. Coordinated with the high affinity for lumichrome, the directed degradation reaction is neutral to the cellular environment and provides an alternative pathway for suppressing uncontrolled riboflavin reactivity. Intriguingly, the different structural and functional properties of a homologous bacterial dodecin suggest that dodecin has different roles in different kingdoms of life.

Dodecin is the key player in flavin homeostasis of archaea.,Grininger M, Staudt H, Johansson P, Wachtveitl J, Oesterhelt D J Biol Chem. 2009 May 8;284(19):13068-76. Epub 2009 Feb 17. PMID:19224924^[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
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vx9"

@@ Line 3: / Line 3: @@
 <StructureSection load='2vx9' size='340' side='right'caption='[[2vx9]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2vx9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hals3 Hals3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VX9 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2VX9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2vx9]] 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=2VX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VX9 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=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=RBF:RIBOFLAVIN'>RBF</scene></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=2vx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vx9 OCA], [http://pdbe.org/2vx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vx9 RCSB], [http://www.ebi.ac.uk/pdbsum/2vx9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vx9 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=2vx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vx9 OCA], [https://pdbe.org/2vx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vx9 RCSB], [https://www.ebi.ac.uk/pdbsum/2vx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vx9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

2vx9

From Proteopedia

Revision as of 11:48, 30 March 2022

H. salinarum dodecin E45A mutant

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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