4aks: Difference between revisions
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== | ==PatG macrocyclase domain== | ||
[[4aks]] is a 2 chain structure with sequence from [ | <StructureSection load='4aks' size='340' side='right'caption='[[4aks]], [[Resolution|resolution]] 2.19Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4aks]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Prochloron_didemni Prochloron didemni]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AKS 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]] 2.19Å</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=4aks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4aks OCA], [https://pdbe.org/4aks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4aks RCSB], [https://www.ebi.ac.uk/pdbsum/4aks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4aks ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q52QJ1_PRODI Q52QJ1_PRODI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Peptide macrocycles are found in many biologically active natural products. Their versatility, resistance to proteolysis and ability to traverse membranes has made them desirable molecules. Although technologies exist to synthesize such compounds, the full extent of diversity found among natural macrocycles has yet to be achieved synthetically. Cyanobactins are ribosomal peptide macrocycles encompassing an extraordinarily diverse range of ring sizes, amino acids and chemical modifications. We report the structure, biochemical characterization and initial engineering of the PatG macrocyclase domain of Prochloron sp. from the patellamide pathway that catalyzes the macrocyclization of linear peptides. The enzyme contains insertions in the subtilisin fold to allow it to recognize a three-residue signature, bind substrate in a preorganized and unusual conformation, shield an acyl-enzyme intermediate from water and catalyze peptide bond formation. The ability to macrocyclize a broad range of nonactivated substrates has wide biotechnology applications. | |||
The mechanism of patellamide macrocyclization revealed by the characterization of the PatG macrocyclase domain.,Koehnke J, Bent A, Houssen WE, Zollman D, Morawitz F, Shirran S, Vendome J, Nneoyiegbe AF, Trembleau L, Botting CH, Smith MC, Jaspars M, Naismith JH Nat Struct Mol Biol. 2012 Jul 15;19(8):767-72. doi: 10.1038/nsmb.2340. Epub 2012 , Jul 15. PMID:22796963<ref>PMID:22796963</ref> | |||
<ref | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4aks" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Prochloron didemni]] | [[Category: Prochloron didemni]] | ||
[[Category: Bent | [[Category: Bent A]] | ||
[[Category: Botting | [[Category: Botting CH]] | ||
[[Category: Houssen | [[Category: Houssen WE]] | ||
[[Category: Jaspars | [[Category: Jaspars M]] | ||
[[Category: Koehnke | [[Category: Koehnke J]] | ||
[[Category: Morawitz | [[Category: Morawitz F]] | ||
[[Category: Naismith | [[Category: Naismith JH]] | ||
[[Category: Nneoyiegbe | [[Category: Nneoyiegbe AF]] | ||
[[Category: Shirran | [[Category: Shirran S]] | ||
[[Category: Smith | [[Category: Smith MCM]] | ||
[[Category: Trembleau | [[Category: Trembleau L]] | ||
[[Category: Vendome | [[Category: Vendome J]] | ||
[[Category: Zollman | [[Category: Zollman D]] | ||
Latest revision as of 11:17, 23 October 2024
PatG macrocyclase domainPatG macrocyclase domain
Structural highlights
FunctionPublication Abstract from PubMedPeptide macrocycles are found in many biologically active natural products. Their versatility, resistance to proteolysis and ability to traverse membranes has made them desirable molecules. Although technologies exist to synthesize such compounds, the full extent of diversity found among natural macrocycles has yet to be achieved synthetically. Cyanobactins are ribosomal peptide macrocycles encompassing an extraordinarily diverse range of ring sizes, amino acids and chemical modifications. We report the structure, biochemical characterization and initial engineering of the PatG macrocyclase domain of Prochloron sp. from the patellamide pathway that catalyzes the macrocyclization of linear peptides. The enzyme contains insertions in the subtilisin fold to allow it to recognize a three-residue signature, bind substrate in a preorganized and unusual conformation, shield an acyl-enzyme intermediate from water and catalyze peptide bond formation. The ability to macrocyclize a broad range of nonactivated substrates has wide biotechnology applications. The mechanism of patellamide macrocyclization revealed by the characterization of the PatG macrocyclase domain.,Koehnke J, Bent A, Houssen WE, Zollman D, Morawitz F, Shirran S, Vendome J, Nneoyiegbe AF, Trembleau L, Botting CH, Smith MC, Jaspars M, Naismith JH Nat Struct Mol Biol. 2012 Jul 15;19(8):767-72. doi: 10.1038/nsmb.2340. Epub 2012 , Jul 15. PMID:22796963[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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