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| | <StructureSection load='2x9i' size='340' side='right'caption='[[2x9i]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2x9i' size='340' side='right'caption='[[2x9i]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x9i]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpprm Bpprm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X9I OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2X9I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x9i]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Prochlorococcus_phage_P-SSM2 Prochlorococcus phage P-SSM2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X9I FirstGlance]. <br> |
| - | </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=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]] 2.2Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2vcl|2vcl]], [[2vck|2vck]], [[2vgr|2vgr]], [[2x9j|2x9j]]</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=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phycoerythrobilin_synthase Phycoerythrobilin synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.7.6 1.3.7.6] </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=2x9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9i OCA], [https://pdbe.org/2x9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x9i RCSB], [https://www.ebi.ac.uk/pdbsum/2x9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x9i ProSAT]</span></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=2x9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9i OCA], [http://pdbe.org/2x9i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x9i RCSB], [http://www.ebi.ac.uk/pdbsum/2x9i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x9i ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PEBS_BPPRM PEBS_BPPRM]] Plays a role in phycoerythrobilin biosynthesis, the red pigment chromophore photosynthetically active biliproteins of the host cyanobacteria. Uses a four-electron reduction to carry out the reactions catalyzed by two enzymes (EC 1.3.7.2 and EC 1.3.7.3) in host. | + | [https://www.uniprot.org/uniprot/PEBS_BPPRM PEBS_BPPRM] Plays a role in phycoerythrobilin biosynthesis, the red pigment chromophore photosynthetically active biliproteins of the host cyanobacteria. Uses a four-electron reduction to carry out the reactions catalyzed by two enzymes (EC 1.3.7.2 and EC 1.3.7.3) in host. |
| | <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: Bpprm]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Phycoerythrobilin synthase]] | + | [[Category: Prochlorococcus phage P-SSM2]] |
| - | [[Category: Busch, A W.U]] | + | [[Category: Busch AWU]] |
| - | [[Category: Frankenberg-Dinkel, N]] | + | [[Category: Frankenberg-Dinkel N]] |
| - | [[Category: Hofmann, E]] | + | [[Category: Hofmann E]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
PEBS_BPPRM Plays a role in phycoerythrobilin biosynthesis, the red pigment chromophore photosynthetically active biliproteins of the host cyanobacteria. Uses a four-electron reduction to carry out the reactions catalyzed by two enzymes (EC 1.3.7.2 and EC 1.3.7.3) in host.
Publication Abstract from PubMed
Phycoerythrobilin (PEB) is a pink-colored open-chain tetrapyrrole molecule found in the cyanobacterial light-harvesting phycobilisome. Within the phycobilisome, PEB is covalently bound via thioether bonds to conserved cysteine residues of the phycobiliprotein subunits. In cyanobacteria, biosynthesis of PEB proceeds via two subsequent two-electron reductions catalyzed by the ferredoxin-dependent bilin reductases (FDBR) PebA and PebB starting from the open-chain tetrapyrrole biliverdin IXalpha. Recently, a new member of the FDBR family was identified in the genome of a marine cyanophage. In contrast to the cyanobacterial enzymes, PEB-synthase (PebS) from cyanophage combines both two-electron reductions for PEB synthesis. Here we show that PebS acts via a substrate radical mechanism and that two conserved aspartate residues at position 105 and 206 are critical for stereospecific substrate protonation and conversion. Based on the crystal structures of both PebS variants and presented biochemical and biophysical data a mechanism for BV conversion to PEB is postulated and discussed with respect to other FDBR family members.
Radical mechanism of cyanophage phycoerythrobilin synthase (PebS).,Busch AW, Reijerse EJ, Lubitz W, Hofmann E, Frankenberg-Dinkel N Biochem J. 2010 Nov 4. PMID:21050180[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Busch AW, Reijerse EJ, Lubitz W, Hofmann E, Frankenberg-Dinkel N. Radical mechanism of cyanophage phycoerythrobilin synthase (PebS). Biochem J. 2010 Nov 4. PMID:21050180 doi:10.1042/BJ20101642
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