|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4m2c' size='340' side='right'caption='[[4m2c]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='4m2c' size='340' side='right'caption='[[4m2c]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4m2c]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_lavendulae_subsp._lavendulae Streptomyces lavendulae subsp. lavendulae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M2C OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=4M2C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4m2c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lavendulae_subsp._lavendulae Streptomyces lavendulae subsp. lavendulae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M2C FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAR:D-ARGININE'>DAR</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAR:D-ARGININE'>DAR</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4m23|4m23]], [[4m25|4m25]], [[4m26|4m26]], [[4m27|4m27]], [[4m2e|4m2e]], [[4m2f|4m2f]], [[4m2g|4m2g]], [[4m2i|4m2i]], [[4m2j|4m2j]], [[4m2k|4m2k]], [[4m2m|4m2m]]</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=4m2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m2c OCA], [https://pdbe.org/4m2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m2c RCSB], [https://www.ebi.ac.uk/pdbsum/4m2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m2c ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4m2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m2c OCA], [http://pdbe.org/4m2c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4m2c RCSB], [http://www.ebi.ac.uk/pdbsum/4m2c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4m2c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/G9MBV2_STRLA G9MBV2_STRLA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 27: |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Streptomyces lavendulae subsp. lavendulae]] | | [[Category: Streptomyces lavendulae subsp. lavendulae]] |
| - | [[Category: Chang, C Y]] | + | [[Category: Chang CY]] |
| - | [[Category: Li, T L]] | + | [[Category: Li TL]] |
| - | [[Category: Liu, Y C]] | + | [[Category: Liu YC]] |
| - | [[Category: Lyu, S Y]] | + | [[Category: Lyu SY]] |
| - | [[Category: Wu, C C]] | + | [[Category: Wu CC]] |
| - | [[Category: Fe binding]]
| + | |
| - | [[Category: Hydroxylase]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
G9MBV2_STRLA
Publication Abstract from PubMed
Streptothricin-F (STT-F), one of the early-discovered antibiotics, consists of three components, a beta-lysine homopolymer, an aminosugar D-gulosamine, and an unusual bicyclic streptolidine. The biosynthesis of streptolidine is a long-lasting but unresolved puzzle. Herein, a combination of genetic/biochemical/structural approaches was used to unravel this problem. The STT gene cluster was first sequenced from a Streptomyces variant BCRC 12163, wherein two gene products OrfP and OrfR were characterized in vitro to be a dihydroxylase and a cyclase, respectively. Thirteen high-resolution crystal structures for both enzymes in different reaction intermediate states were snapshotted to help elucidate their catalytic mechanisms. OrfP catalyzes an Fe(II) -dependent double hydroxylation reaction converting L-Arg into (3R,4R)-(OH)2 -L-Arg via (3S)-OH-L-Arg, while OrfR catalyzes an unusual PLP-dependent elimination/addition reaction cyclizing (3R,4R)-(OH)2 -L-Arg to the six-membered (4R)-OH-capreomycidine. The biosynthetic mystery finally comes to light as the latter product was incorporation into STT-F by a feeding experiment.
Biosynthesis of streptolidine involved two unexpected intermediates produced by a dihydroxylase and a cyclase through unusual mechanisms.,Chang CY, Lyu SY, Liu YC, Hsu NS, Wu CC, Tang CF, Lin KH, Ho JY, Wu CJ, Tsai MD, Li TL Angew Chem Int Ed Engl. 2014 Feb 10;53(7):1943-8. doi: 10.1002/anie.201307989., Epub 2014 Jan 21. PMID:24505011[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chang CY, Lyu SY, Liu YC, Hsu NS, Wu CC, Tang CF, Lin KH, Ho JY, Wu CJ, Tsai MD, Li TL. Biosynthesis of streptolidine involved two unexpected intermediates produced by a dihydroxylase and a cyclase through unusual mechanisms. Angew Chem Int Ed Engl. 2014 Feb 10;53(7):1943-8. doi: 10.1002/anie.201307989., Epub 2014 Jan 21. PMID:24505011 doi:http://dx.doi.org/10.1002/anie.201307989
|
