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'''Unreleased structure'''


The entry 6uly is ON HOLD
==Adenylation domain of a keto acid-selecting NRPS module bound to keto acyl adenylate space group P212121==
<StructureSection load='6uly' size='340' side='right'caption='[[6uly]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6uly]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_stratosphericus_LAMA_585 Bacillus stratosphericus LAMA 585]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ULY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ULY 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=QA7:5-O-{(S)-hydroxy[(4-methyl-2-oxopentanoyl)oxy]phosphoryl}adenosine'>QA7</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6uly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uly OCA], [https://pdbe.org/6uly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uly RCSB], [https://www.ebi.ac.uk/pdbsum/6uly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uly ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Nonribosomal depsipeptides are natural products composed of amino and hydroxy acid residues. The hydroxy acid residues often derive from alpha-keto acids, reduced by ketoreductase domains in the depsipeptide synthetases. Biochemistry and structures reveal the mechanism of discrimination for alpha-keto acids and a remarkable architecture: flanking intact adenylation and ketoreductase domains are sequences separated by &gt;1,100 residues that form a split 'pseudoAsub' domain, structurally important for the depsipeptide module's synthetic cycle.


Authors:  
Structural basis of keto acid utilization in nonribosomal depsipeptide synthesis.,Alonzo DA, Chiche-Lapierre C, Tarry MJ, Wang J, Schmeing TM Nat Chem Biol. 2020 Feb 17. pii: 10.1038/s41589-020-0481-5. doi:, 10.1038/s41589-020-0481-5. PMID:32066969<ref>PMID:32066969</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6uly" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus stratosphericus LAMA 585]]
[[Category: Large Structures]]
[[Category: Alonzo DA]]
[[Category: Chiche-Lapierre C]]
[[Category: Schmeing TM]]
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