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4mfj

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==The crystal structure of acyltransferase==
==The crystal structure of acyltransferase==
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<StructureSection load='4mfj' size='340' side='right' caption='[[4mfj]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
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<StructureSection load='4mfj' size='340' side='right'caption='[[4mfj]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4mfj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MFJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MFJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4mfj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinoplanes_teichomyceticus Actinoplanes teichomyceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MFJ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4mfk|4mfk]], [[4mfl|4mfl]], [[4mfp|4mfp]], [[4mfq|4mfq]], [[4mfs|4mfs]], [[4mft|4mft]], [[4mfw|4mfw]], [[4mfx|4mfx]], [[4mfy|4mfy]], [[4mg0|4mg0]], [[4mg1|4mg1]]</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]] 2.9&#8491;</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mfj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mfj RCSB], [http://www.ebi.ac.uk/pdbsum/4mfj PDBsum]</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=4mfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mfj OCA], [https://pdbe.org/4mfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mfj RCSB], [https://www.ebi.ac.uk/pdbsum/4mfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mfj ProSAT]</span></td></tr>
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<table>
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</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/Q70AY4_ACTTI Q70AY4_ACTTI]
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Teicoplanin A2-2 (Tei)/A40926 is the last-line antibiotic to treat multidrug-resistant Gram-positive bacterial infections, e.g., methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant enterococcus (VRE). This class of antibiotics is powered by the N-acyltransferase (NAT) Orf11*/Dbv8 through N-acylation on glucosamine at the central residue of Tei/A40926 pseudoaglycone. The NAT enzyme possesses enormous value in untapped applications; its advanced development is hampered largely due to a lack of structural information. In this report, we present eight high-resolution X-ray crystallographic unary, binary, and ternary complexes in order to decipher the molecular basis for NAT's functionality. The enzyme undergoes a multistage conformational change upon binding of acyl-CoA, thus allowing the uploading of Tei pseudoaglycone to enable the acyl-transfer reaction to take place in the occlusion between the N- and C-halves of the protein. The acyl moiety of acyl-CoA can be bulky or lengthy, allowing a large extent of diversity in new derivatives that can be formed upon its transfer. Vancomycin/synthetic acyl-N-acetyl cysteamine was not expected to be able to serve as a surrogate for an acyl acceptor/donor, respectively. Most strikingly, NAT can catalyze formation of 2-N,6-O-diacylated or C6--&gt;C2 acyl-substituted Tei analogues through an unusual 1,4-migration mechanism under stoichiometric/solvational reaction control, wherein selected representatives showed excellent biological activities, effectively counteracting major types (VanABC) of VRE.
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Multiple complexes of long aliphatic N-acyltransferases lead to synthesis of 2,6-diacylated/2-acyl-substituted glycopeptide antibiotics, effectively killing vancomycin-resistant enterococcus.,Lyu SY, Liu YC, Chang CY, Huang CJ, Chiu YH, Huang CM, Hsu NS, Lin KH, Wu CJ, Tsai MD, Li TL J Am Chem Soc. 2014 Aug 6;136(31):10989-95. doi: 10.1021/ja504125v. Epub 2014 Jul, 25. PMID:25095906<ref>PMID:25095906</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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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Chang, C Y.]]
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[[Category: Actinoplanes teichomyceticus]]
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[[Category: Huang, C J.]]
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[[Category: Large Structures]]
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[[Category: Li, T L.]]
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[[Category: Chang CY]]
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[[Category: Liu, Y C.]]
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[[Category: Huang CJ]]
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[[Category: Lyu, S Y.]]
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[[Category: Li TL]]
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[[Category: Acyl-coa]]
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[[Category: Liu YC]]
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[[Category: Acyltransferase]]
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[[Category: Lyu SY]]
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[[Category: Gnat]]
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[[Category: Transferase]]
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Current revision

The crystal structure of acyltransferase

PDB ID 4mfj

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