6h1b
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6h1b]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinactinospora_thermotolerans Marinactinospora thermotolerans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H1B FirstGlance]. <br> | <table><tr><td colspan='2'>[[6h1b]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Marinactinospora_thermotolerans Marinactinospora thermotolerans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6H1B FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=EQ2:1-ethanoyl-9~{H}-pyrido[3,4-b]indole-3-carboxylic+acid'>EQ2</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</scene>, <scene name='pdbligand=EQ2:1-ethanoyl-9~{H}-pyrido[3,4-b]indole-3-carboxylic+acid'>EQ2</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=6h1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h1b OCA], [https://pdbe.org/6h1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h1b RCSB], [https://www.ebi.ac.uk/pdbsum/6h1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h1b ProSAT]</span></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=6h1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h1b OCA], [https://pdbe.org/6h1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6h1b RCSB], [https://www.ebi.ac.uk/pdbsum/6h1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6h1b ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/R4R1U5_9ACTN R4R1U5_9ACTN] | [https://www.uniprot.org/uniprot/R4R1U5_9ACTN R4R1U5_9ACTN] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Amide bond formation is one of the most important reactions in pharmaceutical synthetic chemistry. The development of sustainable methods for amide bond formation, including those that are catalyzed by enzymes, is therefore of significant interest. The ATP-dependent amide bond synthetase (ABS) enzyme McbA, from Marinactinospora thermotolerans, catalyzes the formation of amides as part of the biosynthetic pathway towards the marinacarboline secondary metabolites. The reaction proceeds via an adenylate intermediate, with both adenylation and amidation steps catalyzed within one active site. In this study, McbA was applied to the synthesis of pharmaceutical-type amides from a range of aryl carboxylic acids with partner amines provided at 1-5 molar equivalents. The structure of McbA revealed the structural determinants of aryl acid substrate tolerance and differences in conformation associated with the two half reactions catalyzed. The catalytic performance of McbA, coupled with the structure, suggest that this and other ABS enzymes may be engineered for applications in the sustainable synthesis of pharmaceutically relevant (chiral) amides. | ||
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| - | The Broad Aryl Acid Specificity of the Amide Bond Synthetase McbA Suggests Potential for the Biocatalytic Synthesis of Amides.,Petchey M, Cuetos A, Rowlinson B, Dannevald S, Frese A, Sutton PW, Lovelock S, Lloyd RC, Fairlamb IJS, Grogan G Angew Chem Int Ed Engl. 2018 Sep 3;57(36):11584-11588. doi:, 10.1002/anie.201804592. Epub 2018 Aug 7. PMID:30035356<ref>PMID:30035356</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 6h1b" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Structure of amide bond synthetase Mcba K483A mutant from Marinactinospora thermotolerans
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