View source for 7lgn


==Cyanophycin synthetase 1 from T. morbirosei==
<StructureSection load='7lgn' size='340' side='right'caption='[[7lgn]], [[Resolution|resolution]] 3.10&Aring;' 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]] 3.1&#8491;</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]
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7lgn" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Tatumella morbirosei]]
[[Category: Schmeing TM]]
[[Category: Sharon I]]