|
|
| Line 3: |
Line 3: |
| | <StructureSection load='2g18' size='340' side='right'caption='[[2g18]], [[Resolution|resolution]] 2.50Å' scene=''> | | <StructureSection load='2g18' size='340' side='right'caption='[[2g18]], [[Resolution|resolution]] 2.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2g18]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G18 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2G18 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2g18]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Anabaena_sp. Anabaena sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G18 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcyA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1167 Anabaena sp.])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pcyA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1167 Anabaena sp.])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phycocyanobilin:ferredoxin_oxidoreductase Phycocyanobilin:ferredoxin oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.7.5 1.3.7.5] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phycocyanobilin:ferredoxin_oxidoreductase Phycocyanobilin:ferredoxin oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.7.5 1.3.7.5] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g18 OCA], [http://pdbe.org/2g18 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2g18 RCSB], [http://www.ebi.ac.uk/pdbsum/2g18 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2g18 ProSAT]</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=2g18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g18 OCA], [https://pdbe.org/2g18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g18 RCSB], [https://www.ebi.ac.uk/pdbsum/2g18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g18 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PCYA_NOSS1 PCYA_NOSS1]] Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin. Upon overexpression in E.coli with PCB:ferredoxin oxidoreductase, CpeS and either CpcB or PecB permits synthesis of phycocyanin-coupled CpcB or PecB.<ref>PMID:16452471</ref> | + | [[https://www.uniprot.org/uniprot/PCYA_NOSS1 PCYA_NOSS1]] Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin. Upon overexpression in E.coli with PCB:ferredoxin oxidoreductase, CpeS and either CpcB or PecB permits synthesis of phycocyanin-coupled CpcB or PecB.<ref>PMID:16452471</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 30: |
Line 30: |
| | </div> | | </div> |
| | <div class="pdbe-citations 2g18" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 2g18" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Phycocyanobilin:ferredoxin oxidoreductase|Phycocyanobilin:ferredoxin oxidoreductase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[PCYA_NOSS1] Catalyzes the four-electron reduction of biliverdin IX-alpha (2-electron reduction at both the A and D rings); the reaction proceeds via an isolatable 2-electron intermediate, 181,182-dihydrobiliverdin. Upon overexpression in E.coli with PCB:ferredoxin oxidoreductase, CpeS and either CpcB or PecB permits synthesis of phycocyanin-coupled CpcB or PecB.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The X-ray crystal structure of the substrate-free form of phycocyanobilin (PCB)-ferredoxin oxidoreductase (PcyA; EC 1.3.7.5) from the cyanobacterium Nostoc sp. PCC7120 has been solved at 2.5 A resolution. A comparative analysis of this structure with those recently reported for substrate-bound and substrate-free forms of PcyA from the cyanobacterium Synechocystis sp. PCC6803 (Hagiwara et al. (2006) Proc. Natl. Acad. Sci. U.S.A. 103, 27-32; Hagiwara et al. (2006) FEBS Lett. 580, 3823-3828) provides a compelling picture of substrate-induced changes in the PcyA enzyme and the chemical basis of PcyA's catalytic activity. On the basis of these structures and the biochemical analysis of site-directed mutants of Nostoc PcyA, including mutants reported in recent studies (Tu et al. (2006) J. Biol. Chem. 281, 3127-3136) as well as mutants described in this study, a revised mechanism for the PcyA-mediated four-electron reduction of biliverdin IXalpha to 3E/3Z-phycocyanobilin via enzyme-bound bilin radical intermediates is proposed. The mechanistic insight of these studies, along with homology modeling, have provided new insight into the catalytic mechanisms of other members of the ferredoxin-dependent bilin reductase family that are widespread in oxygenic photosynthetic organisms.
Insight into the radical mechanism of phycocyanobilin-ferredoxin oxidoreductase (PcyA) revealed by X-ray crystallography and biochemical measurements.,Tu SL, Rockwell NC, Lagarias JC, Fisher AJ Biochemistry. 2007 Feb 13;46(6):1484-94. Epub 2007 Jan 17. PMID:17279614[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Zhao KH, Su P, Li J, Tu JM, Zhou M, Bubenzer C, Scheer H. Chromophore attachment to phycobiliprotein beta-subunits: phycocyanobilin:cysteine-beta84 phycobiliprotein lyase activity of CpeS-like protein from Anabaena Sp. PCC7120. J Biol Chem. 2006 Mar 31;281(13):8573-81. Epub 2006 Feb 1. PMID:16452471 doi:http://dx.doi.org/10.1074/jbc.M513796200
- ↑ Tu SL, Rockwell NC, Lagarias JC, Fisher AJ. Insight into the radical mechanism of phycocyanobilin-ferredoxin oxidoreductase (PcyA) revealed by X-ray crystallography and biochemical measurements. Biochemistry. 2007 Feb 13;46(6):1484-94. Epub 2007 Jan 17. PMID:17279614 doi:http://dx.doi.org/10.1021/bi062038f
|
