5z83
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='5z83' size='340' side='right' caption='[[5z83]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='5z83' size='340' side='right' caption='[[5z83]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5z83]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z83 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5z83]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_15837 Atcc 15837]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Z83 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5Z83 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gacK, genB1, gntW ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1877 ATCC 15837])</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=5z83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z83 OCA], [http://pdbe.org/5z83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z83 RCSB], [http://www.ebi.ac.uk/pdbsum/5z83 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z83 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=5z83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5z83 OCA], [http://pdbe.org/5z83 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5z83 RCSB], [http://www.ebi.ac.uk/pdbsum/5z83 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5z83 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Gentamicin B (GB), a valuable starting material for the preparation of the semisynthetic aminoglycoside antibiotic isepamicin, is produced in trace amounts by the wild-type Micromonospora echinospora. Though the biosynthetic pathway to GB has remained obscure for decades, we have now identified three hidden pathways to GB production via seven hitherto unknown intermediates in M. echinospora. The narrow substrate specificity of a key glycosyltransferase and the C6'-amination enzymes, in combination with the weak and unsynchronized gene expression of the 2'-deamination enzymes, limits GB production in M. echinospora. The crystal structure of the aminotransferase involved in C6'-amination explains its substrate specificity. Some of the new intermediates displayed similar premature termination codon readthrough activity but with reduced toxicity compared to the natural aminoglycoside G418. This work not only led to the discovery of unknown biosynthetic routes to GB, but also demonstrated the potential to mine new aminoglycosides from nature for drug discovery. | ||
| + | |||
| + | Complete reconstitution of the diverse pathways of gentamicin B biosynthesis.,Ban YH, Song MC, Hwang JY, Shin HL, Kim HJ, Hong SK, Lee NJ, Park JW, Cha SS, Liu HW, Yoon YJ Nat Chem Biol. 2019 Jan 14. pii: 10.1038/s41589-018-0203-4. doi:, 10.1038/s41589-018-0203-4. PMID:30643280<ref>PMID:30643280</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5z83" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 15837]] | ||
[[Category: Cha, S S]] | [[Category: Cha, S S]] | ||
[[Category: Hong, S K]] | [[Category: Hong, S K]] | ||
[[Category: Aminotransferase]] | [[Category: Aminotransferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 09:23, 30 January 2019
Crystal structure of GenB1 from Micromonospora echinospora in complex with PLP (internal aldimine)
| |||||||||||
