4h6v: Difference between revisions
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==Structure of Patellamide maturation protease PatA== | |||
<StructureSection load='4h6v' size='340' side='right'caption='[[4h6v]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4h6v]] is a 1 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=4H6V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H6V 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]] 1.7Å</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=4h6v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h6v OCA], [https://pdbe.org/4h6v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h6v RCSB], [https://www.ebi.ac.uk/pdbsum/4h6v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h6v ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q52QI9_PRODI Q52QI9_PRODI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cyanobactins, a class of ribosomally encoded macrocylic natural products, are biosynthesized through the proteolytic processing and subsequent N-C macrocylization of ribosomal peptide precursors. Macrocylization occurs through a two-step process in which the first protease (PatA) removes the amino terminal flanking sequence from the precursor to yield a free N terminus of the precursor peptide, and the second protease (PatG) removes the C-terminal flanking sequence and then catalyzes the transamidation reaction to yield an N-C cyclized product. Here, we present the crystal structures of the protease domains of PatA and PatG from the patellamide cluster and of PagA from the prenylagaramide cluster. A comparative structural and biochemical analysis of the transamidating PatG protease reveals the presence of a unique structural element distinct from canonical subtilisin proteases, which may facilitate the N-C macrocylization of the peptide substrate. | |||
Structures of cyanobactin maturation enzymes define a family of transamidating proteases.,Agarwal V, Pierce E, McIntosh J, Schmidt EW, Nair SK Chem Biol. 2012 Nov 21;19(11):1411-22. doi: 10.1016/j.chembiol.2012.09.012. PMID:23177196<ref>PMID:23177196</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4h6v" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Prochloron didemni]] | |||
[[Category: Agarwal V]] | |||
[[Category: Nair SK]] | |||
Latest revision as of 07:00, 27 November 2024
Structure of Patellamide maturation protease PatA
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