3pxt: Difference between revisions

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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]] 2.16&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3pxt]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PXT 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=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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=0AF:7-HYDROXY-L-TRYPTOPHAN'>0AF</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3l4m|3l4m]], [[3l4o|3l4o]], [[3orv|3orv]], [[3pxs|3pxs]], [[3pxw|3pxw]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Pd 1222 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266 Paracoccus denitrificans])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Amine_dehydrogenase Amine dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.99.3 1.4.99.3] </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=3pxt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pxt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pxt RCSB], [http://www.ebi.ac.uk/pdbsum/3pxt PDBsum]</span></td></tr>
</table>
<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.


{{STRUCTURE_3pxt|  PDB=3pxt  |  SCENE=  }}
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>


===Crystal Structure of Ferrous CO Adduct of MauG in Complex with Pre-Methylamine Dehydrogenase===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_21355604}}
 
==About this Structure==
[[3pxt]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PXT OCA].


==See Also==
==See Also==
*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:021355604</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Amine dehydrogenase]]
[[Category: Amine dehydrogenase]]
[[Category: Paracoccus denitrificans]]
[[Category: Paracoccus denitrificans]]
[[Category: Goblirsch, B R]]
[[Category: Goblirsch, B R]]
[[Category: Wilmot, C M]]
[[Category: Wilmot, C M]]
[[Category: Yukl, E T.]]
[[Category: Yukl, E T]]
[[Category: Electron transfer]]
[[Category: Electron transfer]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase-electron transport complex]]
[[Category: Oxidoreductase-electron transport complex]]
[[Category: Periplasmic space]]
[[Category: Periplasmic space]]

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