An unusual role of tryptophan in PQQ-containing quinoproteins.
Methanol dehydrogenase is a bacterial quinoprotein containing PQQ at its active site, which is in the centre of a superbarrel structure made up of eight beta-sheets arranged radially as the blades of a propeller. A series of novel tryptophan-docking interactions between the beta-sheets make planar, stabilizing girdles around the periphery of the protein. The tryptophan residues form stacking interactions, and hydrogen bonds through their indole ring NH groups.
Anthony
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Division of Biochemistry and Molecular Biology, School of Biological Sciences, University of Southampton. C.Anthony@soton.ac.uk
D000429:Alcohol Oxidoreductases / Q000737:chemistry* / Q000378:metabolism*; D000595:Amino Acid Sequence; D001665:Binding Sites; D003067:Coenzymes / Q000737:chemistry / Q000378:metabolism; D016384:Consensus Sequence; D008958:Models, Molecular; D045542:PQQ Cofactor; D017433:Protein Structure, Secondary; D015363:Quinolones / Q000737:chemistry / Q000378:metabolism*; D011809:Quinones / Q000737:chemistry / Q000378:metabolism*; D014364:Tryptophan / Q000737:chemistry / Q000378:metabolism*
D003067:Coenzymes; D015363:Quinolones; D011809:Quinones; D045542:PQQ Cofactor; D014364:Tryptophan; D000429:Alcohol Oxidoreductases; C019641:alcohol dehydrogenase (acceptor)