6ulx

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<StructureSection load='6ulx' size='340' side='right'caption='[[6ulx]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
<StructureSection load='6ulx' size='340' side='right'caption='[[6ulx]], [[Resolution|resolution]] 2.31&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ulx]] is a 1 chain structure with sequence from [http://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=6ULX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ULX FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ulx]] is a 1 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=6ULX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ULX FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.31&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C883_1060 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1236481 Bacillus stratosphericus LAMA 585])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
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<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=6ulx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ulx OCA], [http://pdbe.org/6ulx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ulx RCSB], [http://www.ebi.ac.uk/pdbsum/6ulx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ulx ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ulx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ulx OCA], [https://pdbe.org/6ulx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ulx RCSB], [https://www.ebi.ac.uk/pdbsum/6ulx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ulx ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/M5R382_BACIT M5R382_BACIT]
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6ulx" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus stratosphericus lama 585]]
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[[Category: Bacillus stratosphericus LAMA 585]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Alonzo, D A]]
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[[Category: Alonzo DA]]
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[[Category: Chiche-Lapierre, C]]
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[[Category: Chiche-Lapierre C]]
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[[Category: Schmeing, T M]]
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[[Category: Schmeing TM]]
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[[Category: Adenylate]]
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[[Category: Adenylation]]
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[[Category: Adenylation domain]]
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[[Category: Biosynthetic protein]]
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[[Category: Cereulide]]
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[[Category: Depsipeptide]]
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[[Category: Keto acid]]
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[[Category: Ketoacid]]
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[[Category: Natural product]]
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[[Category: Non-ribosomal peptide synthetase]]
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[[Category: Nonribosomal peptide synthetase]]
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[[Category: Nrp]]
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[[Category: Valinomycin]]
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Current revision

Adenylation domain of a keto acid-selecting NRPS module bound to keto acyl adenylate space group P43212

PDB ID 6ulx

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