3l4m: Difference between revisions

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-{{Seed}}
-[[Image:3l4m.jpg|left|200px]]
-<!--
+==Crystal Structure of the MauG/pre-Methylamine Dehydrogenase Complex.==
-The line below this paragraph, containing "STRUCTURE_3l4m", creates the "Structure Box" on the page.
+<StructureSection load='3l4m' size='340' side='right'caption='[[3l4m]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02&#8491;</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>
-{{STRUCTURE_3l4m|  PDB=3l4m  |  SCENE=  }}
+<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.
-===Crystal Structure of the MauG/pre-Methylamine Dehydrogenase Complex.===
+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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3l4m" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-L4M is a 6 chains structure with sequences 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=3L4M OCA].
+*[[Methylamine dehydrogenase|Methylamine dehydrogenase]]
-[[Category: Amine dehydrogenase]]
+*[[Methylamine utilisation protein|Methylamine utilisation protein]]
-[[Category: Paracoccus denitrificans]]
+*[[Methylation utilization protein MauG|Methylation utilization protein MauG]]
-[[Category: Jensen, L M.R.]]
+== References ==
-[[Category: Wilmot, C M.]]
+<references/>
-[[Category: C-heme]]
+__TOC__
-[[Category: Disulfide bond]]
+</StructureSection>
-[[Category: Electron transport]]
+[[Category: Large Structures]]
-[[Category: His-tyr heme]]
+[[Category: Paracoccus denitrificans PD1222]]
-[[Category: Iron]]
+[[Category: Jensen LMR]]
-[[Category: Maug]]
+[[Category: Wilmot CM]]
-[[Category: Metal-binding]]
-[[Category: Methylamine dehydrogenase]]
-[[Category: Oxidoreductase]]
-[[Category: Oxidoreductase-electron transport complex]]
-[[Category: Periplasm]]
-[[Category: Plasmid]]
-[[Category: Quinone cofactor]]
-[[Category: Transport]]
-[[Category: Ttq]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 24 09:04:20 2010''