6omq
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='6omq' size='340' side='right'caption='[[6omq]], [[Resolution|resolution]] 1.86Å' scene=''> | <StructureSection load='6omq' size='340' side='right'caption='[[6omq]], [[Resolution|resolution]] 1.86Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6omq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OMQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OMQ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6omq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13865 Atcc 13865]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OMQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OMQ FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MZD:S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl]+(5beta,7alpha,8alpha,10alpha,11alpha,13alpha)-7-hydroxy-11,16-epoxykaurane-18-thioate'>MZD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MZD:S-[2-({N-[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]-beta-alanyl}amino)ethyl]+(5beta,7alpha,8alpha,10alpha,11alpha,13alpha)-7-hydroxy-11,16-epoxykaurane-18-thioate'>MZD</scene></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=6omq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6omq OCA], [http://pdbe.org/6omq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6omq RCSB], [http://www.ebi.ac.uk/pdbsum/6omq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6omq 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=6omq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6omq OCA], [http://pdbe.org/6omq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6omq RCSB], [http://www.ebi.ac.uk/pdbsum/6omq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6omq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nonheme diiron monooxygenases make up a rapidly growing family of oxygenases that are rarely identified in secondary metabolism. Herein, we report the in vivo, in vitro, and structural characterizations of a nonheme diiron monooxygenase, PtmU3, that installs a C-5 beta-hydroxyl group in the unified biosynthesis of platensimycin and platencin, two highly functionalized diterpenoids that act as potent and selective inhibitors of bacterial and mammalian fatty acid synthases. This hydroxylation sets the stage for the subsequent A-ring cleavage step key to the unique diterpene-derived scaffolds of platensimycin and platencin. PtmU3 adopts an unprecedented triosephosphate isomerase (TIM) barrel structural fold for this class of enzymes and possesses a noncanonical diiron active site architecture with a saturated six-coordinate iron center lacking a mu-oxo bridge. This study reveals the first member of a previously unidentified superfamily of TIM-barrel-fold enzymes for metal-dependent dioxygen activation, with the majority predicted to act on CoA-linked substrates, thus expanding our knowledge of nature's repertoire of nonheme diiron monooxygenases and TIM-barrel-fold enzymes. | ||
| + | |||
| + | Characterization and Crystal Structure of a Nonheme Diiron Monooxygenase Involved in Platensimycin and Platencin Biosynthesis.,Dong LB, Liu YC, Cepeda AJ, Kalkreuter E, Deng MR, Rudolf JD, Chang C, Joachimiak A, Phillips GN Jr, Shen B J Am Chem Soc. 2019 Jul 23. doi: 10.1021/jacs.9b06183. PMID:31291107<ref>PMID:31291107</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6omq" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 13865]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Dong, L B]] | [[Category: Dong, L B]] | ||
Revision as of 07:02, 31 July 2019
Crystal structure of PtmU3 complexed with PTM substrate
| |||||||||||
