6tuk: Difference between revisions
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==Crystal structure of Fdr9== | ==Crystal structure of Fdr9== | ||
<StructureSection load='6tuk' size='340' side='right'caption='[[6tuk]]' scene=''> | <StructureSection load='6tuk' size='340' side='right'caption='[[6tuk]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TUK OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6tuk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermobifida_fusca_YX Thermobifida fusca YX]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6TUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6TUK FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BU3:(R,R)-2,3-BUTANEDIOL'>BU3</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=6tuk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6tuk OCA], [https://pdbe.org/6tuk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6tuk RCSB], [https://www.ebi.ac.uk/pdbsum/6tuk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6tuk ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q47QF8_THEFY Q47QF8_THEFY] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ferredoxin reductase FdR9 from Thermobifida fusca, a member of the oxygenase-coupled NADH-dependent ferredoxin reductase (FNR) family, catalyses electron transfer from NADH to its physiological electron acceptor ferredoxin. It forms part of a putative three-component cytochrome P450 monooxygenase system in T. fusca comprising CYP222A1 and the [3Fe-4S]-cluster ferredoxin Fdx8 as well as FdR9. Here, FdR9 was overexpressed and purified and its crystal structure was determined at 1.9 A resolution. The overall structure of FdR9 is similar to those of other members of the FNR family and is composed of an FAD-binding domain, an NAD-binding domain and a C-terminal domain. Activity measurements with FdR9 confirmed a strong preference for NADH as the cofactor. Comparison of the FAD- and NAD-binding domains of FdR9 with those of other ferredoxin reductases revealed the presence of conserved sequence motifs in the FAD-binding domain as well as several highly conserved residues involved in FAD and NAD cofactor binding. Moreover, the NAD-binding site of FdR9 contains a modified Rossmann-fold motif, GxSxxS, instead of the classical GxGxxG motif. | |||
Expression, purification and crystal structure determination of a ferredoxin reductase from the actinobacterium Thermobifida fusca.,Rodriguez Buitrago JA, Klunemann T, Blankenfeldt W, Schallmey A Acta Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):334-340. doi:, 10.1107/S2053230X2000922X. Epub 2020 Jul 28. PMID:32744244<ref>PMID:32744244</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6tuk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Thermobifida fusca YX]] | |||
[[Category: Blankenfeldt W]] | [[Category: Blankenfeldt W]] | ||
[[Category: Kluenemann T]] | [[Category: Kluenemann T]] | ||
[[Category: Rodriguez A]] | [[Category: Rodriguez A]] | ||
[[Category: Schallmey A]] | [[Category: Schallmey A]] | ||
Latest revision as of 16:09, 24 January 2024
Crystal structure of Fdr9Crystal structure of Fdr9
Structural highlights
FunctionPublication Abstract from PubMedThe ferredoxin reductase FdR9 from Thermobifida fusca, a member of the oxygenase-coupled NADH-dependent ferredoxin reductase (FNR) family, catalyses electron transfer from NADH to its physiological electron acceptor ferredoxin. It forms part of a putative three-component cytochrome P450 monooxygenase system in T. fusca comprising CYP222A1 and the [3Fe-4S]-cluster ferredoxin Fdx8 as well as FdR9. Here, FdR9 was overexpressed and purified and its crystal structure was determined at 1.9 A resolution. The overall structure of FdR9 is similar to those of other members of the FNR family and is composed of an FAD-binding domain, an NAD-binding domain and a C-terminal domain. Activity measurements with FdR9 confirmed a strong preference for NADH as the cofactor. Comparison of the FAD- and NAD-binding domains of FdR9 with those of other ferredoxin reductases revealed the presence of conserved sequence motifs in the FAD-binding domain as well as several highly conserved residues involved in FAD and NAD cofactor binding. Moreover, the NAD-binding site of FdR9 contains a modified Rossmann-fold motif, GxSxxS, instead of the classical GxGxxG motif. Expression, purification and crystal structure determination of a ferredoxin reductase from the actinobacterium Thermobifida fusca.,Rodriguez Buitrago JA, Klunemann T, Blankenfeldt W, Schallmey A Acta Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):334-340. doi:, 10.1107/S2053230X2000922X. Epub 2020 Jul 28. PMID:32744244[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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