This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2x9j

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Structure of the Mutant D206N of Phycoerythrobilin Synthase PebS from the Cyanophage P-SSM2 in complex with bound substrate Biliverdin IXA

Structural highlights

2x9j is a 2 chain structure with sequence from Prochlorococcus phage P-SSM2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.85Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2x9j"

Categories: Large Structures | Prochlorococcus phage P-SSM2 | Busch AWU | Frankenberg-Dinkel N | Hofmann E

@@ Line 3: / Line 3: @@
 <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/Bpprm Bpprm]. 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>
+<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='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>
+</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vcl|2vcl]], [[2x9i|2x9i]], [[2vck|2vck]], [[2vgr|2vgr]]</div></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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phycoerythrobilin_synthase Phycoerythrobilin synthase], with EC number [https://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=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.
+[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 ==
@@ Line 24: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Bpprm]]
 [[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]]

2x9j

From Proteopedia

Current revision

Structure of the Mutant D206N of Phycoerythrobilin Synthase PebS from the Cyanophage P-SSM2 in complex with bound substrate Biliverdin IXA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox