6jpr: Difference between revisions
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The | ==Crystal structure of Phycocyanin from Nostoc sp. R76DM== | ||
<StructureSection load='6jpr' size='340' side='right'caption='[[6jpr]], [[Resolution|resolution]] 2.35Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6jpr]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc Nostoc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JPR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JPR 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]] 2.35Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MEN:N-METHYL+ASPARAGINE'>MEN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=6jpr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jpr OCA], [https://pdbe.org/6jpr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jpr RCSB], [https://www.ebi.ac.uk/pdbsum/6jpr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jpr ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A5H1ZR40_9NOSO A0A5H1ZR40_9NOSO] Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod.[ARBA:ARBA00003579] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The distinct sequence feature and spectral blue-shift (~10 nm) of phycocyanin, isolated from Nostoc sp. R76DM (N-PC), were investigated by phylogenetic and crystallographic analyses. Twelve conserved substitutions in N-PC sequence were found distributed unequally among alpha- and beta-subunit (3 in alpha- and 9 in beta-subunit). The phylogenetic analysis suggested that molecular evolution of alpha- and beta-subunit of Nostoc-phycocyanin is faster than evolution of Nostoc-species. The divergence events seem to have occurred more frequently in beta-subunit, compared to alpha-subunit (relative divergence, 7.38 for alpha-subunit and 9.66 for beta-subunit). Crystal structure of N-PC was solved at 2.35 A resolution to reasonable R-factors (Rwork/RFree = 0.199/0.248). Substitutions congregate near interface of two alphabeta-monomer in N-PC trimer and are of compensatory nature. Six of the substitutions in beta-subunit may be involved in maintaining topology of beta-subunit, one in inter-monomer interaction and one in interaction with linker-protein. The beta153Cys-attached chromophore adopts high-energy conformational state resulting due to reduced coplanarity of B- and C-pyrrole rings. Distortion in chromophore conformation can result in blue-shift in N-PC spectral properties. N-PC showed significant in-vitro and in-vivo antioxidant activity comparable with other phycocyanin. Since Nostoc-species constitute a distinct phylogenetic clade, the present structure would provide a better template to build a model for phycocyanins of these species. | |||
Phylogenetic and crystallographic analysis of Nostoc phycocyanin having blue-shifted spectral properties.,Sonani RR, Rastogi RP, Patel SN, Chaubey MG, Singh NK, Gupta GD, Kumar V, Madamwar D Sci Rep. 2019 Jul 8;9(1):9863. doi: 10.1038/s41598-019-46288-4. PMID:31285455<ref>PMID:31285455</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6jpr" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Kumar | ==See Also== | ||
[[Category: | *[[Phycocyanin|Phycocyanin]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Nostoc]] | |||
[[Category: Gupta GD]] | |||
[[Category: Kumar V]] | |||
[[Category: Madamwar D]] | |||
[[Category: Patel SN]] | |||
[[Category: Rastogi RP]] | |||
[[Category: Sonani RR]] | |||
Latest revision as of 13:18, 22 November 2023
Crystal structure of Phycocyanin from Nostoc sp. R76DMCrystal structure of Phycocyanin from Nostoc sp. R76DM
Structural highlights
FunctionA0A5H1ZR40_9NOSO Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex (phycobilisome, PBS). Phycocyanin is the major phycobiliprotein in the PBS rod.[ARBA:ARBA00003579] Publication Abstract from PubMedThe distinct sequence feature and spectral blue-shift (~10 nm) of phycocyanin, isolated from Nostoc sp. R76DM (N-PC), were investigated by phylogenetic and crystallographic analyses. Twelve conserved substitutions in N-PC sequence were found distributed unequally among alpha- and beta-subunit (3 in alpha- and 9 in beta-subunit). The phylogenetic analysis suggested that molecular evolution of alpha- and beta-subunit of Nostoc-phycocyanin is faster than evolution of Nostoc-species. The divergence events seem to have occurred more frequently in beta-subunit, compared to alpha-subunit (relative divergence, 7.38 for alpha-subunit and 9.66 for beta-subunit). Crystal structure of N-PC was solved at 2.35 A resolution to reasonable R-factors (Rwork/RFree = 0.199/0.248). Substitutions congregate near interface of two alphabeta-monomer in N-PC trimer and are of compensatory nature. Six of the substitutions in beta-subunit may be involved in maintaining topology of beta-subunit, one in inter-monomer interaction and one in interaction with linker-protein. The beta153Cys-attached chromophore adopts high-energy conformational state resulting due to reduced coplanarity of B- and C-pyrrole rings. Distortion in chromophore conformation can result in blue-shift in N-PC spectral properties. N-PC showed significant in-vitro and in-vivo antioxidant activity comparable with other phycocyanin. Since Nostoc-species constitute a distinct phylogenetic clade, the present structure would provide a better template to build a model for phycocyanins of these species. Phylogenetic and crystallographic analysis of Nostoc phycocyanin having blue-shifted spectral properties.,Sonani RR, Rastogi RP, Patel SN, Chaubey MG, Singh NK, Gupta GD, Kumar V, Madamwar D Sci Rep. 2019 Jul 8;9(1):9863. doi: 10.1038/s41598-019-46288-4. PMID:31285455[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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