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| | ==THE ACTIVE SITE STRUCTURE OF METHYLAMINE DEHYDROGENASE: HYDRAZINES IDENTIFY C6 AS THE REACTIVE SITE OF THE TRYPTOPHAN DERIVED QUINONE COFACTOR== | | ==THE ACTIVE SITE STRUCTURE OF METHYLAMINE DEHYDROGENASE: HYDRAZINES IDENTIFY C6 AS THE REACTIVE SITE OF THE TRYPTOPHAN DERIVED QUINONE COFACTOR== |
| - | <StructureSection load='2mad' size='340' side='right' caption='[[2mad]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='2mad' size='340' side='right'caption='[[2mad]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mad]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25364 Atcc 25364]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mad 1mad]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MAD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mad]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Paracoccus_versutus Paracoccus versutus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1mad 1mad]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MAD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MAD FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylamine_dehydrogenase_(amicyanin) Methylamine dehydrogenase (amicyanin)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.1 1.4.9.1] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></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=2mad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mad OCA], [http://pdbe.org/2mad PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mad RCSB], [http://www.ebi.ac.uk/pdbsum/2mad PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mad ProSAT]</span></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=2mad FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mad OCA], [https://pdbe.org/2mad PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mad RCSB], [https://www.ebi.ac.uk/pdbsum/2mad PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mad ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DHML_PARVE DHML_PARVE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. [[http://www.uniprot.org/uniprot/DHMH_PARVE DHMH_PARVE]] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. | + | [https://www.uniprot.org/uniprot/DHML_PARVE DHML_PARVE] Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 25364]] | + | [[Category: Large Structures]] |
| - | [[Category: Hol, W G.J]] | + | [[Category: Paracoccus versutus]] |
| - | [[Category: Huizinga, E G]] | + | [[Category: Hol WGJ]] |
| - | [[Category: Vellieux, F M.D]] | + | [[Category: Huizinga EG]] |
| | + | [[Category: Vellieux FMD]] |
| Structural highlights
Function
DHML_PARVE Methylamine dehydrogenase carries out the oxidation of methylamine. Electrons are passed from methylamine dehydrogenase to amicyanin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
To identify the reactive part of the orthoquinone function of the tryptophan-derived cofactor found in methylamine dehydrogenase (MADH), we have determined the crystal structures of MADH from Thiobacillus versutus inhibited by methylhydrazine and (2,2,2-trifluoroethyl)hydrazine. Extra electron density attached to C6 of the tryptophyl tryptophanquinone cofactor shows that this atom and not C7 is the reactive part of the ortho-quinone moiety. The density retained after hydrazine inhibition is much less extensive than expected, however, suggesting that partial breakdown of the inhibitors after reaction with the cofactor may take place. A detailed description is presented of the cofactor environment in an improved model of MADH which now includes information from the recently determined gene sequence of the cofactor-containing subunit [Ubbink, M., van Kleef, M.A.G., Kleinjan, D., Hoitink, C.W.G., Huitema, F., Beintema, J.J., Duine, J.A., & Canters, G.W. (1991) Eur. J. Biochem. 202, 1003-1012]. We hypothesize that Asp76 is responsible for proton abstraction from the alpha-carbon of the substrate during catalysis.
Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor.,Huizinga EG, van Zanten BA, Duine JA, Jongejan JA, Huitema F, Wilson KS, Hol WG Biochemistry. 1992 Oct 13;31(40):9789-95. PMID:1390754[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Huizinga EG, van Zanten BA, Duine JA, Jongejan JA, Huitema F, Wilson KS, Hol WG. Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor. Biochemistry. 1992 Oct 13;31(40):9789-95. PMID:1390754
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