7lgn: Difference between revisions
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New page: '''Unreleased structure''' The entry 7lgn is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Cyanophycin synthetase 1 from T. morbirosei== | |||
<StructureSection load='7lgn' size='340' side='right'caption='[[7lgn]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7lgn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tatumella_morbirosei Tatumella morbirosei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LGN 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]] 3.1Å</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=7lgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lgn OCA], [https://pdbe.org/7lgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lgn RCSB], [https://www.ebi.ac.uk/pdbsum/7lgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lgn ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A095T5Z8_9GAMM A0A095T5Z8_9GAMM] 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> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7lgn" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Tatumella morbirosei]] | |||
[[Category: Schmeing TM]] | |||
[[Category: Sharon I]] | |||
