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| <StructureSection load='7lgm' size='340' side='right'caption='[[7lgm]], [[Resolution|resolution]] 4.40Å' scene=''> | | <StructureSection load='7lgm' size='340' side='right'caption='[[7lgm]], [[Resolution|resolution]] 4.40Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[7lgm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aciad Aciad]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LGM FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LGM FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></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]] 4.4Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cphA, ACIAD1279 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=62977 ACIAD])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</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=7lgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lgm OCA], [https://pdbe.org/7lgm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lgm RCSB], [https://www.ebi.ac.uk/pdbsum/7lgm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lgm ProSAT]</span></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=7lgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7lgm OCA], [https://pdbe.org/7lgm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7lgm RCSB], [https://www.ebi.ac.uk/pdbsum/7lgm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7lgm ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
| |
| [[https://www.uniprot.org/uniprot/Q6FCQ7_ACIAD Q6FCQ7_ACIAD]] 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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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| 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.
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| 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>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 7lgm" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Aciad]]
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Haque, A S]] | | [[Category: Haque AS]] |
| [[Category: Lahiri, I]] | | [[Category: Lahiri I]] |
| [[Category: Leschziner, A]] | | [[Category: Leschziner A]] |
| [[Category: Schmeing, T M]] | | [[Category: Schmeing TM]] |
| [[Category: Sharon, I]] | | [[Category: Sharon I]] |
| [[Category: Atp-grasp]]
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| [[Category: Cpha1]]
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| [[Category: Cyanophycin]]
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| [[Category: Ligase]]
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