8fun: Difference between revisions
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==Enzymatically Active, Mn/Fe Metallated Form of AibH1H2== | |||
<StructureSection load='8fun' size='340' side='right'caption='[[8fun]], [[Resolution|resolution]] 2.24Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8fun]] 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=8FUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FUN 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=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=8fun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fun OCA], [https://pdbe.org/8fun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fun RCSB], [https://www.ebi.ac.uk/pdbsum/8fun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fun 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 8fun" 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
Enzymatically Active, Mn/Fe Metallated Form of AibH1H2
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