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< | ==Crystal Structure of the MauG/pre-Methylamine Dehydrogenase Complex.== | ||
<StructureSection load='3l4m' size='340' side='right'caption='[[3l4m]], [[Resolution|resolution]] 2.02Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3l4m]] 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=3L4M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L4M FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02Å</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=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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=3l4m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l4m OCA], [https://pdbe.org/3l4m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l4m RCSB], [https://www.ebi.ac.uk/pdbsum/3l4m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l4m ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A1BBA0_PARDP A1BBA0_PARDP] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l4/3l4m_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3l4m ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
MauG is a diheme enzyme responsible for the posttranslational modification of two tryptophan residues to form the tryptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrogenase (MADH). MauG converts preMADH, containing monohydroxylated betaTrp57, to fully functional MADH by catalyzing the insertion of a second oxygen atom into the indole ring and covalently linking betaTrp57 to betaTrp108. We have solved the x-ray crystal structure of MauG complexed with preMADH to 2.1 angstroms. The c-type heme irons and the nascent TTQ site are separated by long distances over which electron transfer must occur to achieve catalysis. In addition, one of the hemes has an atypical His-Tyr axial ligation. The crystalline protein complex is catalytically competent; upon addition of hydrogen peroxide, MauG-dependent TTQ synthesis occurs. | |||
In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex.,Jensen LM, Sanishvili R, Davidson VL, Wilmot CM Science. 2010 Mar 12;327(5971):1392-4. PMID:20223990<ref>PMID:20223990</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3l4m" 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: | [[Category: Paracoccus denitrificans PD1222]] | ||
[[Category: | [[Category: Jensen LMR]] | ||
[[Category: | [[Category: Wilmot CM]] | ||
[[Category: | |||
Latest revision as of 13:07, 6 November 2024
Crystal Structure of the MauG/pre-Methylamine Dehydrogenase Complex.Crystal Structure of the MauG/pre-Methylamine Dehydrogenase Complex.
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMauG is a diheme enzyme responsible for the posttranslational modification of two tryptophan residues to form the tryptophan tryptophylquinone (TTQ) cofactor of methylamine dehydrogenase (MADH). MauG converts preMADH, containing monohydroxylated betaTrp57, to fully functional MADH by catalyzing the insertion of a second oxygen atom into the indole ring and covalently linking betaTrp57 to betaTrp108. We have solved the x-ray crystal structure of MauG complexed with preMADH to 2.1 angstroms. The c-type heme irons and the nascent TTQ site are separated by long distances over which electron transfer must occur to achieve catalysis. In addition, one of the hemes has an atypical His-Tyr axial ligation. The crystalline protein complex is catalytically competent; upon addition of hydrogen peroxide, MauG-dependent TTQ synthesis occurs. In crystallo posttranslational modification within a MauG/pre-methylamine dehydrogenase complex.,Jensen LM, Sanishvili R, Davidson VL, Wilmot CM Science. 2010 Mar 12;327(5971):1392-4. PMID:20223990[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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