5fcx: Difference between revisions
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==Structure of Anabaena (Nostoc) sp. PCC 7120 Red Carotenoid Protein binding canthaxanthin== | |||
<StructureSection load='5fcx' size='340' side='right'caption='[[5fcx]], [[Resolution|resolution]] 3.21Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5fcx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FCX 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]] 3.206Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=45D:BETA,BETA-CAROTENE-4,4-DIONE'>45D</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=5fcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fcx OCA], [https://pdbe.org/5fcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fcx RCSB], [https://www.ebi.ac.uk/pdbsum/5fcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fcx ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8YXT8_NOSS1 Q8YXT8_NOSS1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Using a phylogenomic approach, we have identified and subclassified a new family of carotenoid-binding proteins. These proteins have sequence homology to the N-terminal domain (NTD) of the Orange Carotenoid Protein (OCP), and are referred to as Helical Carotenoid Proteins (HCPs). These proteins comprise at least nine distinct clades and are found in diverse organisms, frequently as multiple paralogs representing the distinct clades. These seem to be out-paralogs maintained from ancient duplications associated with subfunctionalization. All of the HCPs share conservation of the residues for carotenoid binding and we confirm that carotenoid binding is a fundamental property of HCPs. We solved two crystal structures of the Nostoc sp. PCC 7120 HCP1 protein, each binding a different carotenoid, suggesting that the proteins flexibly bind a range of carotenoids. Based on a comprehensive phylogenetic analysis, we propose that one of the HCP subtypes is likely the evolutionary ancestor of the NTD of the OCP, which arose following a domain fusion event. However, we predict that the majority of HCPs have functions distinct from the NTD of the OCP. Our results demonstrate that the HCPs are a new family of functionally diverse carotenoid-binding proteins found among ecophysiologically diverse cyanobacteria. | |||
Structure, Diversity, and Evolution of a New Family of Soluble Carotenoid Binding Proteins in Cyanobacteria.,Melnicki MR, Leverenz RL, Sutter M, Lopez-Igual R, Wilson A, Pawlowski EG, Perreau F, Kirilovsky D, Kerfeld CA Mol Plant. 2016 Jul 5. pii: S1674-2052(16)30101-0. doi:, 10.1016/j.molp.2016.06.009. PMID:27392608<ref>PMID:27392608</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5fcx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Nostoc sp. PCC 7120 = FACHB-418]] | |||
[[Category: Kerfeld CA]] | |||
[[Category: Leverenz RL]] | |||
[[Category: Sutter M]] | |||
Latest revision as of 09:46, 19 July 2023
Structure of Anabaena (Nostoc) sp. PCC 7120 Red Carotenoid Protein binding canthaxanthinStructure of Anabaena (Nostoc) sp. PCC 7120 Red Carotenoid Protein binding canthaxanthin
Structural highlights
FunctionPublication Abstract from PubMedUsing a phylogenomic approach, we have identified and subclassified a new family of carotenoid-binding proteins. These proteins have sequence homology to the N-terminal domain (NTD) of the Orange Carotenoid Protein (OCP), and are referred to as Helical Carotenoid Proteins (HCPs). These proteins comprise at least nine distinct clades and are found in diverse organisms, frequently as multiple paralogs representing the distinct clades. These seem to be out-paralogs maintained from ancient duplications associated with subfunctionalization. All of the HCPs share conservation of the residues for carotenoid binding and we confirm that carotenoid binding is a fundamental property of HCPs. We solved two crystal structures of the Nostoc sp. PCC 7120 HCP1 protein, each binding a different carotenoid, suggesting that the proteins flexibly bind a range of carotenoids. Based on a comprehensive phylogenetic analysis, we propose that one of the HCP subtypes is likely the evolutionary ancestor of the NTD of the OCP, which arose following a domain fusion event. However, we predict that the majority of HCPs have functions distinct from the NTD of the OCP. Our results demonstrate that the HCPs are a new family of functionally diverse carotenoid-binding proteins found among ecophysiologically diverse cyanobacteria. Structure, Diversity, and Evolution of a New Family of Soluble Carotenoid Binding Proteins in Cyanobacteria.,Melnicki MR, Leverenz RL, Sutter M, Lopez-Igual R, Wilson A, Pawlowski EG, Perreau F, Kirilovsky D, Kerfeld CA Mol Plant. 2016 Jul 5. pii: S1674-2052(16)30101-0. doi:, 10.1016/j.molp.2016.06.009. PMID:27392608[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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