6ulz: Difference between revisions

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OCA

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-'''Unreleased structure'''
-The entry 6ulz is ON HOLD
+==Adenylation domain of the initiation module of LgrA mutant P483M==
+<StructureSection load='6ulz' size='340' side='right'caption='[[6ulz]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6ulz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brevibacillus_parabrevis Brevibacillus parabrevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ULZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ULZ 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]] 3.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APC:DIPHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>APC</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=KIV:3-METHYL-2-OXOBUTANOIC+ACID'>KIV</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=6ulz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ulz OCA], [https://pdbe.org/6ulz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ulz RCSB], [https://www.ebi.ac.uk/pdbsum/6ulz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ulz ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LGRA_BREPA LGRA_BREPA] Activates valine (or leucine, but much less frequently), and then glycine and catalyzes the formation of the peptide bond in the first step of peptide synthesis. This enzyme may also play a role in N-formylation of the first amino acid residue in the synthesized dipeptide.
+<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 6ulz" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Linear gramicidin synthase|Linear gramicidin synthase]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Brevibacillus parabrevis]]
+[[Category: Large Structures]]
+[[Category: Alonzo DA]]
+[[Category: Chiche-Lapierre C]]
+[[Category: Schmeing TM]]