6uly
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==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]] 2.30Å' 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]] 2.3Å</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 >1,100 residues that form a split 'pseudoAsub' domain, structurally important for the depsipeptide module's synthetic cycle. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </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]] | ||
Current revision
Adenylation domain of a keto acid-selecting NRPS module bound to keto acyl adenylate space group P212121
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