4h6w
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4h6w is ON HOLD Authors: Nair, S.K., Agarwal, V. Description: Structure of Prenylagaramide maturation protease PagA) |
|||
| (6 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Prenylagaramide maturation protease PagA== | |
| + | <StructureSection load='4h6w' size='340' side='right'caption='[[4h6w]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4h6w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Planktothrix_agardhii_NIES-596 Planktothrix agardhii NIES-596]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H6W 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]] 2.45Å</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=4h6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h6w OCA], [https://pdbe.org/4h6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h6w RCSB], [https://www.ebi.ac.uk/pdbsum/4h6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h6w ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/F5B6Y7_PLAAG F5B6Y7_PLAAG] | ||
| + | <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 4h6w" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Planktothrix agardhii NIES-596]] | ||
| + | [[Category: Agarwal V]] | ||
| + | [[Category: Nair SK]] | ||
Current revision
Structure of Prenylagaramide maturation protease PagA
| |||||||||||
