View source for 2x9j


==Structure of the Mutant D206N of Phycoerythrobilin Synthase PebS from the Cyanophage P-SSM2 in complex with bound substrate Biliverdin IXA==
<StructureSection load='2x9j' size='340' side='right'caption='[[2x9j]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2x9j]] is a 2 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=2X9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X9J 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]] 1.85&#8491;</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></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=2x9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9j OCA], [https://pdbe.org/2x9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x9j RCSB], [https://www.ebi.ac.uk/pdbsum/2x9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x9j ProSAT]</span></td></tr>
</table>
== Function ==
[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;">
== 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<ref>PMID:21050180</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2x9j" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Prochlorococcus phage P-SSM2]]
[[Category: Busch AWU]]
[[Category: Frankenberg-Dinkel N]]
[[Category: Hofmann E]]