7lgq
From Proteopedia
(Difference between revisions)
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- | ==== | + | ==Cyanophycin synthetase 1 from Synechocystis sp. UTEX2470 with ATP and 8x(Asp-Arg)-Asn== |
- | <StructureSection load='7lgq' size='340' side='right'caption='[[7lgq]]' scene=''> | + | <StructureSection load='7lgq' size='340' side='right'caption='[[7lgq]], [[Resolution|resolution]] 2.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7lgq]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6714 Synechocystis sp. PCC 6714] 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=7LGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LGQ FirstGlance]. <br> |
- | </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=7lgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lgq OCA], [https://pdbe.org/7lgq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lgq RCSB], [https://www.ebi.ac.uk/pdbsum/7lgq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lgq ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.7Å</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7lgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lgq OCA], [https://pdbe.org/7lgq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lgq RCSB], [https://www.ebi.ac.uk/pdbsum/7lgq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lgq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/A0A068N621_SYNY4 A0A068N621_SYNY4] Catalyzes the ATP-dependent polymerization of arginine and aspartate to multi-L-arginyl-poly-L-aspartic acid (cyanophycin; a water-insoluble reserve polymer).[ARBA:ARBA00003184] | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Cyanophycin is a natural biopolymer produced by a wide range of bacteria, consisting of a chain of poly-L-Asp residues with L-Arg residues attached to the beta-carboxylate sidechains by isopeptide bonds. Cyanophycin is synthesized from ATP, aspartic acid and arginine by a homooligomeric enzyme called cyanophycin synthetase (CphA1). CphA1 has domains that are homologous to glutathione synthetases and muramyl ligases, but no other structural information has been available. Here, we present cryo-electron microscopy and X-ray crystallography structures of cyanophycin synthetases from three different bacteria, including cocomplex structures of CphA1 with ATP and cyanophycin polymer analogs at 2.6 A resolution. These structures reveal two distinct tetrameric architectures, show the configuration of active sites and polymer-binding regions, indicate dynamic conformational changes and afford insight into catalytic mechanism. Accompanying biochemical interrogation of substrate binding sites, catalytic centers and oligomerization interfaces combine with the structures to provide a holistic understanding of cyanophycin biosynthesis. | ||
+ | |||
+ | Structures and function of the amino acid polymerase cyanophycin synthetase.,Sharon I, Haque AS, Grogg M, Lahiri I, Seebach D, Leschziner AE, Hilvert D, Schmeing TM Nat Chem Biol. 2021 Oct;17(10):1101-1110. doi: 10.1038/s41589-021-00854-y. Epub, 2021 Aug 12. PMID:34385683<ref>PMID:34385683</ref> | ||
+ | |||
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 7lgq" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Synechocystis sp. PCC 6714]] |
+ | [[Category: Synthetic construct]] | ||
+ | [[Category: Grogg M]] | ||
+ | [[Category: Hilvert D]] | ||
+ | [[Category: Schmeing TM]] | ||
+ | [[Category: Sharon I]] |
Current revision
Cyanophycin synthetase 1 from Synechocystis sp. UTEX2470 with ATP and 8x(Asp-Arg)-Asn
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