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http://purl.uniprot.org/citations/11502180http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11502180http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11502180http://www.w3.org/2000/01/rdf-schema#comment"The structure of an active mutant of (S)-mandelate dehydrogenase (MDH-GOX2) from Pseudomonas putida has been determined at 2.15 A resolution. The membrane-associated flavoenzyme (S)-mandelate dehydrogenase (MDH) catalyzes the oxidation of (S)-mandelate to give a flavin hydroquinone intermediate which is subsequently reoxidized by an organic oxidant residing in the membrane. The enzyme was rendered soluble by replacing its 39-residue membrane-binding peptide segment with a corresponding 20-residue segment from its soluble homologue, glycolate oxidase (GOX). Because of their amphipathic nature and peculiar solubilization properties, membrane proteins are notoriously difficult to crystallize, yet represent a large fraction of the proteins encoded by genomes currently being deciphered. Here we present the first report of such a structure in which an internal membrane-binding segment has been replaced, leading to successful crystallization of the fully active enzyme in the absence of detergents. This approach may have general application to other membrane-bound proteins. The overall fold of the molecule is that of a TIM barrel, and it forms a tight tetramer within the crystal lattice that has circular 4-fold symmetry. The structure of MDH-GOX2 reveals how this molecule can interact with a membrane, although it is limited by the absence of a membrane-binding segment. MDH-GOX2 and GOX adopt similar conformations, yet they retain features characteristic of membrane and globular proteins, respectively. MDH-GOX2 has a distinctly electropositive surface capable of interacting with the membrane, while the opposite surface is largely electronegative. GOX shows no such pattern. MDH appears to form a new class of monotopic integral membrane protein that interacts with the membrane through coplanar electrostatic binding surfaces and hydrophobic interactions, thus combining features of both the prostaglandin synthase/squaline-hopine cyclase and the C-2 coagulation factor domain classes of membrane proteins."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.org/dc/terms/identifier"doi:10.1021/bi010938k"xsd:string
http://purl.uniprot.org/citations/11502180http://purl.org/dc/terms/identifier"doi:10.1021/bi010938k"xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/author"Mathews F.S."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/author"Mathews F.S."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/author"Sukumar N."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/author"Sukumar N."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/author"Xu Y."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/author"Xu Y."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/author"Gatti D.L."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/author"Gatti D.L."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/author"Mitra B."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/author"Mitra B."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/pages"9870-9878"xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/pages"9870-9878"xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/title"Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/title"Structure of an active soluble mutant of the membrane-associated (S)-mandelate dehydrogenase."xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/volume"40"xsd:string
http://purl.uniprot.org/citations/11502180http://purl.uniprot.org/core/volume"40"xsd:string
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