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==X-Ray Crystal Structure of Allophycocyanin from Synechococcus elongatus PCC 7942== | |||
<StructureSection load='4f0u' size='340' side='right'caption='[[4f0u]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4f0u]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechococcus_elongatus_PCC_7942_=_FACHB-805 Synechococcus elongatus PCC 7942 = FACHB-805]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F0U FirstGlance]. <br> | |||
</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=MEN:N-METHYL+ASPARAGINE'>MEN</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=4f0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f0u OCA], [https://pdbe.org/4f0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f0u RCSB], [https://www.ebi.ac.uk/pdbsum/4f0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f0u ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q31RG0_SYNE7 Q31RG0_SYNE7] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
X-ray crystal structures of the isolated phycobiliprotein components of the phycobilisome have provided high resolution details to the description of this light harvesting complex at different levels of complexity and detail. The linker-independent assembly of trimers into hexamers in crystal lattices of previously determined structures has been observed in almost all of the phycocyanin (PC) and allophycocyanin (APC) structures available in the Protein Data Bank. In this paper we describe the X-ray crystal structures of PC and APC from Synechococcus elongatus sp. PCC 7942, PC from Synechocystis sp. PCC 6803 and PC from Thermosynechococcus vulcanus crystallized in the presence of urea. All five structures are highly similar to other PC and APC structures on the levels of subunits, monomers and trimers. The Synechococcus APC forms a unique loose hexamer that may show the structural requirements for core assembly and rod attachment. While the Synechococcus PC assembles into the canonical hexamer, it does not further assemble into rods. Unlike most PC structures, the Synechocystis PC fails to form hexamers. Addition of low concentrations of urea to T. vulcanus PC inhibits this proteins propensity to form hexamers, resulting in a crystal lattice composed of trimers. The molecular source of these differences in assembly and their relevance to the phycobilisome structure is discussed. | |||
Allophycocyanin and phycocyanin crystal structures reveal facets of phycobilisome assembly.,Marx A, Adir N Biochim Biophys Acta. 2013 Mar;1827(3):311-8. doi: 10.1016/j.bbabio.2012.11.006. , Epub 2012 Nov 28. PMID:23201474<ref>PMID:23201474</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4f0u" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Allophycocyanin 3D structures|Allophycocyanin 3D structures]] | ||
[[Category: Synechococcus elongatus]] | == References == | ||
[[Category: Adir | <references/> | ||
[[Category: Marx | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]] | |||
[[Category: Adir N]] | |||
[[Category: Marx A]] | |||
Latest revision as of 07:27, 7 October 2022
X-Ray Crystal Structure of Allophycocyanin from Synechococcus elongatus PCC 7942X-Ray Crystal Structure of Allophycocyanin from Synechococcus elongatus PCC 7942
Structural highlights
FunctionPublication Abstract from PubMedX-ray crystal structures of the isolated phycobiliprotein components of the phycobilisome have provided high resolution details to the description of this light harvesting complex at different levels of complexity and detail. The linker-independent assembly of trimers into hexamers in crystal lattices of previously determined structures has been observed in almost all of the phycocyanin (PC) and allophycocyanin (APC) structures available in the Protein Data Bank. In this paper we describe the X-ray crystal structures of PC and APC from Synechococcus elongatus sp. PCC 7942, PC from Synechocystis sp. PCC 6803 and PC from Thermosynechococcus vulcanus crystallized in the presence of urea. All five structures are highly similar to other PC and APC structures on the levels of subunits, monomers and trimers. The Synechococcus APC forms a unique loose hexamer that may show the structural requirements for core assembly and rod attachment. While the Synechococcus PC assembles into the canonical hexamer, it does not further assemble into rods. Unlike most PC structures, the Synechocystis PC fails to form hexamers. Addition of low concentrations of urea to T. vulcanus PC inhibits this proteins propensity to form hexamers, resulting in a crystal lattice composed of trimers. The molecular source of these differences in assembly and their relevance to the phycobilisome structure is discussed. Allophycocyanin and phycocyanin crystal structures reveal facets of phycobilisome assembly.,Marx A, Adir N Biochim Biophys Acta. 2013 Mar;1827(3):311-8. doi: 10.1016/j.bbabio.2012.11.006. , Epub 2012 Nov 28. PMID:23201474[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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