3pxt
From Proteopedia
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- | [[Image:3pxt.png|left|200px]] | ||
- | < | + | ==Crystal Structure of Ferrous CO Adduct of MauG in Complex with Pre-Methylamine Dehydrogenase== |
- | + | <StructureSection load='3pxt' size='340' side='right'caption='[[3pxt]], [[Resolution|resolution]] 2.16Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[3pxt]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_denitrificans_PD1222 Paracoccus denitrificans PD1222]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PXT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PXT FirstGlance]. <br> | |
- | or | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.16Å</td></tr> |
- | -- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0AF:7-HYDROXY-L-TRYPTOPHAN'>0AF</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG6:1-(2-METHOXY-ETHOXY)-2-{2-[2-(2-METHOXY-ETHOXY]-ETHOXY}-ETHANE'>PG6</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=3pxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pxt OCA], [https://pdbe.org/3pxt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pxt RCSB], [https://www.ebi.ac.uk/pdbsum/3pxt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pxt ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/MAUG_PARDP MAUG_PARDP] Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH. | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | MauG is a diheme enzyme responsible for the post-translational formation of the catalytic tryptophan tryptophylquinone (TTQ) cofactor in methylamine dehydrogenase (MADH). MauG can utilize hydrogen peroxide, or molecular oxygen and reducing equivalents, to complete this reaction via a catalytic bis-Fe(IV) intermediate. Crystal structures of diferrous, Fe(II)-CO, and Fe(II)-NO forms of MauG in complex with its preMADH substrate have been determined and compared to one another as well as to the structure of the resting diferric MauG-preMADH complex. CO and NO each bind exclusively to the 5-coordinate high-spin heme with no change in ligation of the 6-coordinate low-spin heme. These structures reveal likely roles for amino acid residues in the distal pocket of the high-spin heme in oxygen binding and activation. Glu113 is implicated in the protonation of heme-bound diatomic oxygen intermediates in promoting cleavage of the O-O bond. Pro107 is shown to change conformation on the binding of each ligand and may play a steric role in oxygen activation by positioning the distal oxygen near Glu113. Gln103 is in a position to provide a hydrogen bond to the Fe(IV) horizontal lineO moiety that may account for the unusual stability of this species in MauG. | ||
- | + | Crystal Structures of CO and NO Adducts of MauG in Complex with Pre-Methylamine Dehydrogenase: Implications for the Mechanism of Dioxygen Activation.,Yukl ET, Goblirsch BR, Davidson VL, Wilmot CM Biochemistry. 2011 Mar 16. PMID:21355604<ref>PMID:21355604</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 3pxt" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Methylamine dehydrogenase|Methylamine dehydrogenase]] | |
- | + | *[[Methylamine utilisation protein|Methylamine utilisation protein]] | |
- | + | *[[Methylation utilization protein MauG|Methylation utilization protein MauG]] | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | [[ | + | </StructureSection> |
- | + | [[Category: Large Structures]] | |
- | == | + | [[Category: Paracoccus denitrificans PD1222]] |
- | < | + | [[Category: Goblirsch BR]] |
- | [[Category: | + | [[Category: Wilmot CM]] |
- | [[Category: Paracoccus denitrificans]] | + | [[Category: Yukl ET]] |
- | [[Category: Goblirsch | + | |
- | [[Category: Wilmot | + | |
- | [[Category: Yukl | + |
Current revision
Crystal Structure of Ferrous CO Adduct of MauG in Complex with Pre-Methylamine Dehydrogenase
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