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| <StructureSection load='5awv' size='340' side='right'caption='[[5awv]], [[Resolution|resolution]] 1.93Å' scene=''> | | <StructureSection load='5awv' size='340' side='right'caption='[[5awv]], [[Resolution|resolution]] 1.93Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5awv]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_39727 Atcc 39727]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4k3t 4k3t] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wdx 2wdx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AWV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5awv]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinoplanes_teichomyceticus Actinoplanes teichomyceticus] and [https://en.wikipedia.org/wiki/Nonomuraea_gerenzanensis Nonomuraea gerenzanensis]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4k3t 4k3t] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2wdx 2wdx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AWV FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=N1L:2-AMINO-2-DEOXY-BETA-D-GLUCOPYRANURONIC+ACID'>N1L</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=T55:8-METHYLNONANOIC+ACID'>T55</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]] 1.93Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=3FG:(2S)-AMINO(3,5-DIHYDROXYPHENYL)ETHANOIC+ACID'>3FG</scene>, <scene name='pdbligand=3MY:3-CHLORO-D-TYROSINE'>3MY</scene>, <scene name='pdbligand=GHP:(2R)-AMINO(4-HYDROXYPHENYL)ETHANOIC+ACID'>GHP</scene>, <scene name='pdbligand=OMY:(BETAR)-3-CHLORO-BETA-HYDROXY-L-TYROSINE'>OMY</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3FG:(2S)-AMINO(3,5-DIHYDROXYPHENYL)ETHANOIC+ACID'>3FG</scene>, <scene name='pdbligand=3MY:3-CHLORO-D-TYROSINE'>3MY</scene>, <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GHP:(2R)-AMINO(4-HYDROXYPHENYL)ETHANOIC+ACID'>GHP</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=N1L:2-AMINO-2-DEOXY-BETA-D-GLUCOPYRANURONIC+ACID'>N1L</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OMY:(BETAR)-3-CHLORO-BETA-HYDROXY-L-TYROSINE'>OMY</scene>, <scene name='pdbligand=T55:8-METHYLNONANOIC+ACID'>T55</scene></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dbv29 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=93944 ATCC 39727])</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=5awv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awv OCA], [https://pdbe.org/5awv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5awv RCSB], [https://www.ebi.ac.uk/pdbsum/5awv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5awv ProSAT]</span></td></tr> |
- | <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=5awv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5awv OCA], [http://pdbe.org/5awv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5awv RCSB], [http://www.ebi.ac.uk/pdbsum/5awv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5awv ProSAT]</span></td></tr> | + | |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/Q7WZ62_9ACTN Q7WZ62_9ACTN] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Atcc 39727]] | + | [[Category: Actinoplanes teichomyceticus]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Li, T L]] | + | [[Category: Nonomuraea gerenzanensis]] |
- | [[Category: Liu, Y C]] | + | [[Category: Li TL]] |
- | [[Category: Oxidoreductase-antibiotic complex]] | + | [[Category: Liu YC]] |
| Structural highlights
5awv is a 12 chain structure with sequence from Actinoplanes teichomyceticus and Nonomuraea gerenzanensis. This structure supersedes the now removed PDB entries 4k3t and 2wdx. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| Method: | X-ray diffraction, Resolution 1.93Å |
Ligands: | , , , , , , , , , |
Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
Q7WZ62_9ACTN
Publication Abstract from PubMed
In the search for new efficacious antibiotics, biosynthetic engineering offers attractive opportunities to introduce minor alterations to antibiotic structures that may overcome resistance. Dbv29, a flavin-containing oxidase, catalyzes the four-electron oxidation of a vancomycin-like glycopeptide to yield A40926. Structural and biochemical examination of Dbv29 now provides insights into residues that govern flavinylation and activity, protein conformation and reaction mechanism. In particular, the serendipitous discovery of a reaction intermediate in the crystal structure led us to identify an unexpected opportunity to intercept the normal enzyme mechanism at two different points to create new teicoplanin analogs. Using this method, we synthesized families of antibiotic analogs with amidated and aminated lipid chains, some of which showed marked potency and efficacy against multidrug resistant pathogens. This method offers a new strategy for the development of chemical diversity to combat antibacterial resistance.
Interception of teicoplanin oxidation intermediates yields new antimicrobial scaffolds.,Liu YC, Li YS, Lyu SY, Hsu LJ, Chen YH, Huang YT, Chan HC, Huang CJ, Chen GH, Chou CC, Tsai MD, Li TL Nat Chem Biol. 2011 May;7(5):304-9. Epub 2011 Apr 10. PMID:21478878[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu YC, Li YS, Lyu SY, Hsu LJ, Chen YH, Huang YT, Chan HC, Huang CJ, Chen GH, Chou CC, Tsai MD, Li TL. Interception of teicoplanin oxidation intermediates yields new antimicrobial scaffolds. Nat Chem Biol. 2011 May;7(5):304-9. Epub 2011 Apr 10. PMID:21478878 doi:10.1038/nchembio.556
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