4m23: Difference between revisions
New page: '''Unreleased structure''' The entry 4m23 is ON HOLD Authors: Chang, C.Y., Liu, Y.C., Lyu, S.Y., Wu, C.C., Li, T.L. Description: Crystal structure of non-heme iron oxygenase OrfP |
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The | ==Crystal structure of non-heme iron oxygenase OrfP== | ||
<StructureSection load='4m23' size='340' side='right'caption='[[4m23]], [[Resolution|resolution]] 1.76Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4m23]] 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=4M23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4M23 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76Å</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=4m23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4m23 OCA], [https://pdbe.org/4m23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4m23 RCSB], [https://www.ebi.ac.uk/pdbsum/4m23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4m23 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/G9MBV2_STRLA G9MBV2_STRLA] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:24505011</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4m23" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Hydroxylases 3D structures|Hydroxylases 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptomyces lavendulae subsp. lavendulae]] | |||
[[Category: Chang CY]] | |||
[[Category: Li TL]] | |||
[[Category: Liu YC]] | |||
[[Category: Lyu SY]] | |||
[[Category: Wu CC]] | |||
Latest revision as of 17:39, 8 November 2023
Crystal structure of non-heme iron oxygenase OrfPCrystal structure of non-heme iron oxygenase OrfP
Structural highlights
FunctionPublication Abstract from PubMedStreptothricin-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 AlsoReferences
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