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2g18

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==Crystal Structure of Nostoc sp. 7120 phycocyanobilin:ferredoxin oxidoreductase (PcyA) Apoprotein==
==Crystal Structure of Nostoc sp. 7120 phycocyanobilin:ferredoxin oxidoreductase (PcyA) Apoprotein==
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<StructureSection load='2g18' size='340' side='right' caption='[[2g18]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='2g18' size='340' side='right'caption='[[2g18]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<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>
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<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>
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<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>
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<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>
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<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]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/2g18_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g1/2g18_consurf.spt"</scriptWhenChecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
<text>to colour the structure by Evolutionary Conservation</text>
<text>to colour the structure by Evolutionary Conservation</text>
</jmolCheckbox>
</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2g18 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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<ref>PMID:17279614</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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</div>
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*[[Phycocyanobilin:ferredoxin oxidoreductase|Phycocyanobilin:ferredoxin oxidoreductase]]
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<div class="pdbe-citations 2g18" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Anabaena sp]]
[[Category: Anabaena sp]]
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[[Category: Phycocyanobilin:ferredoxin oxidoreductase]]
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[[Category: Large Structures]]
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[[Category: Fisher, A J]]
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[[Category: Fisher AJ]]
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[[Category: Lagarias, J C]]
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[[Category: Lagarias JC]]
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[[Category: Tu, S L]]
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[[Category: Tu S-L]]
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[[Category: Alpha-beta-alpha sandwich]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal Structure of Nostoc sp. 7120 phycocyanobilin:ferredoxin oxidoreductase (PcyA) Apoprotein

PDB ID 2g18

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