View source for 8fxi


==Cryo-EM structure of Stanieria sp. CphA2 in complex with ADPCP and 4x(beta-Asp-Arg)==
<StructureSection load='8fxi' size='340' side='right'caption='[[8fxi]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8fxi]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Stanieria_sp._NIES-3757 Stanieria sp. NIES-3757] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FXI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FXI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=7ID:L-beta-aspartyl-L-arginine'>7ID</scene>, <scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=YHZ:[[[(2~{R},3~{S},4~{R},5~{S})-5-[[(4-azanylpyrimidin-5-yl)amino]methyl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]methylphosphonic+acid'>YHZ</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=8fxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fxi OCA], [https://pdbe.org/8fxi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fxi RCSB], [https://www.ebi.ac.uk/pdbsum/8fxi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fxi ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
Cyanophycin is a natural polymer composed of a poly-aspartate backbone with arginine attached to each of the aspartate sidechains. Produced by a wide range of bacteria, which mainly use it as a store of fixed nitrogen, it has many promising industrial applications. Cyanophycin can be synthesized from the amino acids Asp and Arg by the widespread cyanophycin synthetase 1 (CphA1), or from the dipeptide beta-Asp-Arg by the cyanobacterial enzyme cyanophycin synthetase 2 (CphA2). CphA2 enzymes display a range of oligomeric states, from dimers to dodecamers. Recently, the crystal structure of a CphA2 dimer was solved but could not be obtained in complex with substrate. Here, we report cryo-EM structures of the hexameric CphA2 from Stanieria sp. at ~2.8 A resolution, both with and without ATP analog and cyanophycin. The structures show a two-fold symmetrical, trimer-of-dimers hexameric architecture, and substrate-binding interactions that are similar to those of CphA1. Mutagenesis experiments demonstrate the importance of several conserved substrate-binding residues. We also find that a Q416A/R528G double mutation prevents hexamer formation and use this double mutant to show that hexamerization augments the rate of cyanophycin synthesis. Together, these results increase our mechanistic understanding of how an interesting green polymer is biosynthesized.

Structure and function of a hexameric cyanophycin synthetase 2.,Markus LMD, Sharon I, Munro K, Grogg M, Hilvert D, Strauss M, Schmeing TM Protein Sci. 2023 Jul;32(7):e4685. doi: 10.1002/pro.4685. PMID:37222490<ref>PMID:37222490</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8fxi" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Stanieria sp. NIES-3757]]
[[Category: Synthetic construct]]
[[Category: Markus LM]]
[[Category: Schmeing TM]]
[[Category: Sharon I]]
[[Category: Strauss M]]