8fuo
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Fe-bound AibH1H2== | |
| + | <StructureSection load='8fuo' size='340' side='right'caption='[[8fuo]], [[Resolution|resolution]] 2.43Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8fuo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_wratislaviensis_NBRC_100605 Rhodococcus wratislaviensis NBRC 100605]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FUO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FUO FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></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=8fuo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fuo OCA], [https://pdbe.org/8fuo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fuo RCSB], [https://www.ebi.ac.uk/pdbsum/8fuo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fuo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A402C2V4_RHOWR A0A402C2V4_RHOWR] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Manganese cofactors activate strong chemical bonds in many essential enzymes. Yet very few manganese-dependent enzymes are known to functionalize ubiquitous carbon-hydrogen (C-H) bonds, and those that catalyze this important reaction display limited intrinsic reactivity. Herein, we report that the 2-aminoisobutyric acid hydroxylase from Rhodococcus wratislaviensis requires manganese to functionalize a C-H bond possessing a bond dissociation enthalpy (BDE) exceeding 100 kcal/mol. Structural and spectroscopic studies of this enzyme reveal a redox-active, heterobimetallic manganese-iron active site that utilizes a manganese ion at the locus for O (2) activation and substrate coordination. Accordingly, this enzyme represents the first documented Mn-dependent monooxygenase in biology. Related proteins are widespread in microorganisms suggesting that many uncharacterized monooxygenases may utilize manganese-containing cofactors to accomplish diverse biological tasks. | ||
| - | + | Enzymatic Hydroxylation of Aliphatic C-H Bonds by a Mn/Fe Cofactor.,Powell MM, Rao G, Britt RD, Rittle J bioRxiv. 2023 Mar 11:2023.03.10.532131. doi: 10.1101/2023.03.10.532131. Preprint. PMID:36945426<ref>PMID:36945426</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Powell | + | <div class="pdbe-citations 8fuo" style="background-color:#fffaf0;"></div> |
| - | [[Category: Rittle | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Rhodococcus wratislaviensis NBRC 100605]] | ||
| + | [[Category: Powell MM]] | ||
| + | [[Category: Rittle J]] | ||
Revision as of 06:31, 7 April 2023
Fe-bound AibH1H2
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