8bp7: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Unreleased structure'''
-The entry 8bp7 is ON HOLD
+==Citrate-bound hexamer of Synechococcus elongatus citrate synthase==
+<StructureSection load='8bp7' size='340' side='right'caption='[[8bp7]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8bp7]] 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=8BP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BP7 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]] 2.71&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8bp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bp7 OCA], [https://pdbe.org/8bp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bp7 RCSB], [https://www.ebi.ac.uk/pdbsum/8bp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bp7 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q31QM5_SYNE7 Q31QM5_SYNE7]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Fractals are patterns that are self-similar across multiple length-scales(1). Macroscopic fractals are common in nature(2-4); however, so far, molecular assembly into fractals is restricted to synthetic systems(5-12). Here we report the discovery of a natural protein, citrate synthase from the cyanobacterium Synechococcus elongatus, which self-assembles into Sierpinski triangles. Using cryo-electron microscopy, we reveal how the fractal assembles from a hexameric building block. Although different stimuli modulate the formation of fractal complexes and these complexes can regulate the enzymatic activity of citrate synthase in vitro, the fractal may not serve a physiological function in vivo. We use ancestral sequence reconstruction to retrace how the citrate synthase fractal evolved from non-fractal precursors, and the results suggest it may have emerged as a harmless evolutionary accident. Our findings expand the space of possible protein complexes and demonstrate that intricate and regulatable assemblies can evolve in a single substitution.
-Authors:
+Emergence of fractal geometries in the evolution of a metabolic enzyme.,Sendker FL, Lo YK, Heimerl T, Bohn S, Persson LJ, Mais CN, Sadowska W, Paczia N, Nussbaum E, Del Carmen Sanchez Olmos M, Forchhammer K, Schindler D, Erb TJ, Benesch JLP, Marklund EG, Bange G, Schuller JM, Hochberg GKA Nature. 2024 Apr;628(8009):894-900. doi: 10.1038/s41586-024-07287-2. Epub 2024 , Apr 10. PMID:38600380<ref>PMID:38600380</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 8bp7" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Synechococcus elongatus PCC 7942 = FACHB-805]]
+[[Category: Bange G]]
+[[Category: Mais C-N]]
+[[Category: Sendker F]]