2x9o: Difference between revisions
New page: '''Unreleased structure''' The entry 2x9o is ON HOLD Authors: Busch, A.W.U., Frankenberg-Dinkel, N., Hofmann, E. Description: STRUCTURE OF 15, 16-DIHYDROBILIVERDIN:FERREDOXIN OXIDOREDU... |
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==STRUCTURE OF 15, 16- DIHYDROBILIVERDIN:FERREDOXIN OXIDOREDUCTASE (PebA)== | |||
<StructureSection load='2x9o' size='340' side='right'caption='[[2x9o]], [[Resolution|resolution]] 1.55Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x9o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_sp._WH_8020 Synechococcus sp. WH 8020]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X9O FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.55Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BLA:BILIVERDINE+IX+ALPHA'>BLA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=2x9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9o OCA], [https://pdbe.org/2x9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x9o RCSB], [https://www.ebi.ac.uk/pdbsum/2x9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x9o ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PEBA_SYNPY PEBA_SYNPY] Catalyzes the two-electron reduction of biliverdin IX-alpha at the C15 methine bridge. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
PEB (phycoerythrobilin) is one of the major open-chain tetrapyrrole molecules found in cyanobacterial light-harvesting phycobiliproteins. In these organisms, two enzymes of the ferredoxin-dependent bilin reductase family work in tandem to reduce BV (biliverdin IXalpha) to PEB. In contrast, a single cyanophage-encoded enzyme of the same family has been identified to catalyse the identical reaction. Using UV-visible and EPR spectroscopy we investigated the two individual cyanobacterial enzymes PebA [15,16-DHBV (dihydrobiliverdin):ferredoxin oxidoreductase] and PebB (PEB:ferredoxin oxidoreductase) showing that the two subsequent reactions catalysed by the phage enzyme PebS (PEB synthase) are clearly dissected in the cyanobacterial versions. Although a highly conserved aspartate residue is critical for both reductions, a second conserved aspartate residue is only involved in the A-ring reduction of the tetrapyrrole in PebB and PebS. The crystal structure of PebA from Synechococcus sp. WH8020 in complex with its substrate BV at a 1.55 A (1 A=0.1 nm) resolution revealed further insight into the understanding of enzyme evolution and function. Based on the structure it becomes obvious that in addition to the importance of certain catalytic residues, the shape of the active site and consequently the binding of the substrate highly determines the catalytic properties. | |||
Structural and mechanistic insight into the ferredoxin-mediated two-electron reduction of bilins.,Busch AW, Reijerse EJ, Lubitz W, Frankenberg-Dinkel N, Hofmann E Biochem J. 2011 Oct 15;439(2):257-64. doi: 10.1042/BJ20110814. PMID:21729003<ref>PMID:21729003</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2x9o" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synechococcus sp. WH 8020]] | |||
[[Category: Busch AWU]] | |||
[[Category: Frankenberg-Dinkel N]] | |||
[[Category: Hofmann E]] | |||
Latest revision as of 15:45, 17 January 2024
STRUCTURE OF 15, 16- DIHYDROBILIVERDIN:FERREDOXIN OXIDOREDUCTASE (PebA)STRUCTURE OF 15, 16- DIHYDROBILIVERDIN:FERREDOXIN OXIDOREDUCTASE (PebA)
Structural highlights
FunctionPEBA_SYNPY Catalyzes the two-electron reduction of biliverdin IX-alpha at the C15 methine bridge. Publication Abstract from PubMedPEB (phycoerythrobilin) is one of the major open-chain tetrapyrrole molecules found in cyanobacterial light-harvesting phycobiliproteins. In these organisms, two enzymes of the ferredoxin-dependent bilin reductase family work in tandem to reduce BV (biliverdin IXalpha) to PEB. In contrast, a single cyanophage-encoded enzyme of the same family has been identified to catalyse the identical reaction. Using UV-visible and EPR spectroscopy we investigated the two individual cyanobacterial enzymes PebA [15,16-DHBV (dihydrobiliverdin):ferredoxin oxidoreductase] and PebB (PEB:ferredoxin oxidoreductase) showing that the two subsequent reactions catalysed by the phage enzyme PebS (PEB synthase) are clearly dissected in the cyanobacterial versions. Although a highly conserved aspartate residue is critical for both reductions, a second conserved aspartate residue is only involved in the A-ring reduction of the tetrapyrrole in PebB and PebS. The crystal structure of PebA from Synechococcus sp. WH8020 in complex with its substrate BV at a 1.55 A (1 A=0.1 nm) resolution revealed further insight into the understanding of enzyme evolution and function. Based on the structure it becomes obvious that in addition to the importance of certain catalytic residues, the shape of the active site and consequently the binding of the substrate highly determines the catalytic properties. Structural and mechanistic insight into the ferredoxin-mediated two-electron reduction of bilins.,Busch AW, Reijerse EJ, Lubitz W, Frankenberg-Dinkel N, Hofmann E Biochem J. 2011 Oct 15;439(2):257-64. doi: 10.1042/BJ20110814. PMID:21729003[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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