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==COMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDS==
==COMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDS==
<StructureSection load='4b2h' size='340' side='right' caption='[[4b2h]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='4b2h' size='340' side='right' caption='[[4b2h]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4b2h]] is a 1 chain structure with sequence from [http://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=4B2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B2H FirstGlance]. <br>
<table><tr><td colspan='2'>[[4b2h]] 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=4B2H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4B2H FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C3F:3-[7,8-DIMETHYL-2,4-BIS(OXIDANYLIDENE)BENZO[G]PTERIDIN-10-YL]PROPYLCARBAMIC+ACID'>C3F</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C3F:3-[7,8-DIMETHYL-2,4-BIS(OXIDANYLIDENE)BENZO[G]PTERIDIN-10-YL]PROPYLCARBAMIC+ACID'>C3F</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=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cc8|2cc8]], [[2ccb|2ccb]], [[2vx9|2vx9]], [[4b2l|4b2l]], [[4b2k|4b2k]], [[4b2j|4b2j]], [[4b2m|4b2m]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cc8|2cc8]], [[2ccb|2ccb]], [[2vx9|2vx9]], [[4b2l|4b2l]], [[4b2k|4b2k]], [[4b2j|4b2j]], [[4b2m|4b2m]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4b2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b2h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4b2h RCSB], [http://www.ebi.ac.uk/pdbsum/4b2h PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4b2h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b2h OCA], [http://pdbe.org/4b2h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4b2h RCSB], [http://www.ebi.ac.uk/pdbsum/4b2h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4b2h ProSAT]</span></td></tr>
</table>
</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> 
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Halobacterium salinarum r1]]
[[Category: Hals3]]
[[Category: Grininger, M]]
[[Category: Grininger, M]]
[[Category: Heidel, B]]
[[Category: Heidel, B]]

Revision as of 21:32, 4 August 2016

COMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDSCOMPLEXES OF DODECIN WITH FLAVIN AND FLAVIN-LIKE LIGANDS

Structural highlights

4b2h 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]

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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

4b2h, resolution 1.60Å

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