View source for 6iyk


==The structure of EntE with 2-nitrobenzoyl adenylate analog==
<StructureSection load='6iyk' size='340' side='right'caption='[[6iyk]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6iyk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_1303 Escherichia coli 1303]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6IYK 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]] 2.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B1U:5-O-[(2-nitrobenzene-1-carbonyl)sulfamoyl]adenosine'>B1U</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=6iyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6iyk OCA], [https://pdbe.org/6iyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6iyk RCSB], [https://www.ebi.ac.uk/pdbsum/6iyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6iyk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ENTE_ECOLI ENTE_ECOLI] Activates the carboxylate group of 2,3-dihydroxy-benzoate (2,3-DHB), via ATP-dependent PPi exchange reactions, to the acyladenylate. Then, catalyzes the acylation of holo-EntB with 2,3-DHB adenylate, preparing that molecule for amide bond formation with L-serine.
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6iyk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli 1303]]
[[Category: Large Structures]]
[[Category: Ishikawa F]]
[[Category: Miyanaga A]]