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• W2896957283 abstract "Monotopic proteins are underrepresented in the PDB, with only 25 nonredundant structures currently constituting ∼0.06% of known structures. Many monotopic membrane proteins are homologous to soluble counterparts and use common structural features to embed shallowly in the membrane. Selected monotopic proteins engage more deeply in the membrane (e.g., associating via reentrant-helical domains). Monotopic enzymes are purposed for catalysis of reactions involving hydrophobic or amphiphilic substrates not readily soluble in water. The active sites of monotopic enzymes may be at the membrane surface or distal to it, and the requirement for hydrophobic substrate extraction is dictated by the substrate and the relative orientations of the active site and the membrane. Association of multiple monotopic enzymes in pathways can be advantageously applied in the assembly of complex glycoconjugates. Monotopic membrane proteins, classified by topology, are proteins that embed into a single face of the membrane. These proteins are generally underrepresented in the Protein Data Bank (PDB), but the past decade of research has revealed new examples that allow the description of generalizable features. This Opinion article summarizes shared characteristics including oligomerization states, modes of membrane association, mechanisms of interaction with hydrophobic or amphiphilic substrates, and homology to soluble folds. We also discuss how associations of monotopic enzymes in pathways can be used to promote substrate specificity and product composition. These examples highlight the challenges in structure determination specific to this class of proteins, but also the promise of new understanding from future study of these proteins that reside at the interface. Monotopic membrane proteins, classified by topology, are proteins that embed into a single face of the membrane. These proteins are generally underrepresented in the Protein Data Bank (PDB), but the past decade of research has revealed new examples that allow the description of generalizable features. This Opinion article summarizes shared characteristics including oligomerization states, modes of membrane association, mechanisms of interaction with hydrophobic or amphiphilic substrates, and homology to soluble folds. We also discuss how associations of monotopic enzymes in pathways can be used to promote substrate specificity and product composition. These examples highlight the challenges in structure determination specific to this class of proteins, but also the promise of new understanding from future study of these proteins that reside at the interface. a molecule, protein segment, or protein having both hydophobic and hydrophilic components. a membrane protein that spans the membrane bilayer a single time; sometimes referred to as a ‘single-pass’ transmembrane protein. an enzyme that catalyzes the transfer of a sugar from an activated sugar donor, commonly a nucleoside diphosphate derivative, to an acceptor such as another sugar or a lipid. members of the same protein family. a protein that is inserted into the membrane and can be solubilized only by detergent. two structurally and funtionally similar proteins with nonidentical sequences due to encoding by different genes or splicing variations. a membrane protein that does not span the membrane bilayer, but rather enters and exits on a single face of the membrane bilayer. a curated web resource providing information on the position of proteins in membranes. Included in the database is output from the PPM server. members of the same protein family having the same function but occuring in different organisms. members of the same protein family having different functions. a protein associated with the membrane surface in a manner that can be dissociated by the addition of high salt. an enzyme that catalyzes the transfer of a phosphosugar from an activated sugar donor, commonly a nucleoside diphosphate derivative, to an acceptor substrate such as a polyprenol phosphate. a linear long-chain alcohol featuring greater than six isoprene units (branched five-carbon units) of either cis or trans configuration. a membrane protein that spans the membrane bilayer multiple times. calculates rotational and translational positions of transmembrane and peripheral proteins in the membrane using the PDB coordinate files as input. a discontinuous hydrophobic helix that enters and exits on a single face of the membrane bilayer. a fold characterized by repeating motifs of α-helix–β-strand–α-helix secondary structure elements where the β-strands together form a parallel β-sheet. an algorithm to predict transmembrane helices in proteins using a hidden Markov model." @default.
• W2896957283 created "2018-10-26" @default.
• W2896957283 creator A5005385287 @default.
• W2896957283 creator A5057579902 @default.
• W2896957283 creator A5062358325 @default.
• W2896957283 creator A5068838774 @default.
• W2896957283 date "2019-01-01" @default.
• W2896957283 modified "2023-10-16" @default.
• W2896957283 title "Monotopic Membrane Proteins Join the Fold" @default.
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• W2896957283 doi "https://doi.org/10.1016/j.tibs.2018.09.013" @default.
• W2896957283 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6309722" @default.
• W2896957283 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30337134" @default.
• W2896957283 hasPublicationYear "2019" @default.
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