6iyk: Difference between revisions
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The | ==The structure of EntE with 2-nitrobenzoyl adenylate analog== | ||
<StructureSection load='6iyk' size='340' side='right'caption='[[6iyk]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6iyk]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IYK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IYK FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=B1U:5-O-[(2-nitrobenzene-1-carbonyl)sulfamoyl]adenosine'>B1U</scene></td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/(2,3-dihydroxybenzoyl)adenylate_synthase (2,3-dihydroxybenzoyl)adenylate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.58 2.7.7.58] </span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6iyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iyk OCA], [http://pdbe.org/6iyk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6iyk RCSB], [http://www.ebi.ac.uk/pdbsum/6iyk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6iyk ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Adenylation (A) domains act as the gatekeepers of non-ribosomal peptide synthetases (NRPSs) ensuring the activation and thioesterification of the correct amino acid/aryl acid building blocks. Aryl acid building blocks are most commonly observed in iron-chelating siderophores, but are not limited to them. The non-ribosomal codes toward aryl acid substrates are poorly understood. Very little is known about the reprogramming of aryl acid A-domains. Here we show that a single asparagine-to-glycine mutation in an aryl acid A-domain creates novel enzyme specificities toward a wide range of non-native aryl acids. The engineered catalyst is capable of activating the non-native aryl acids functionalized with nitro, cyano, bromo, and iodo, even though no enzymatic activity of wild-type enzyme was observed toward these substrates. Co-crystal structures with non-hydrolysable aryl-AMP analogues revealed the origins of substrate promiscuity expansion, highlighting an enlarged substrate binding pocket of the enzyme. Our finding may be exploited to produce diversified aryl acid-containing natural products and serve as a template for further directed evolution in combinatorial biosynthesis. | |||
An engineered aryl acid adenylation domain with a capacious active site microenvironment.,Ishikawa F, Miyanaga A, Kitayama H, Nakamura S, Nakanishi I, Kudo F, Eguchi T, Tanabe G Angew Chem Int Ed Engl. 2019 Apr 3. doi: 10.1002/anie.201900318. PMID:30945421<ref>PMID:30945421</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6iyk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Ishikawa, F]] | |||
[[Category: Miyanaga, A]] | |||
[[Category: Adenylation]] | |||
[[Category: Ligase]] | |||
[[Category: Non-ribosomal peptide biosynthesis]] | |||
