Search Results - "Wilmot, Carrie M."

Quaternary Structure Defines a Large Class of Amyloid-β Oligomers Neutralized by Sequestration by Liu, Peng, Reed, Miranda N., Kotilinek, Linda A., Grant, Marianne K.O., Forster, Colleen L., Qiang, Wei, Shapiro, Samantha L., Reichl, John H., Chiang, Angie C.A., Jankowsky, Joanna L., Wilmot, Carrie M., Cleary, James P., Zahs, Kathleen R., Ashe, Karen H.

“…The accumulation of amyloid-β (Aβ) as amyloid fibrils and toxic oligomers is an important step in the development of Alzheimer’s disease (AD). However, there…”
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Structural Studies of Hydroxylamine Oxidoreductase Reveal a Unique Heme Cofactor and a Previously Unidentified Interaction Partner by Cedervall, Peder, Hooper, Alan B, Wilmot, Carrie M

“…Hydroxylamine oxidoreductase (HAO) is a 24-heme homotrimeric enzyme that catalyzes the conversion of hydroxylamine to nitrite in nitrifying bacteria: a key…”
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Discovery of Hydroxylase Activity for PqqB Provides a Missing Link in the Pyrroloquinoline Quinone Biosynthetic Pathway by Koehn, Eric M, Latham, John A, Armand, Tara, Evans, Robert L, Tu, Xiongying, Wilmot, Carrie M, Iavarone, Anthony T, Klinman, Judith P

“…Understanding the biosynthesis of cofactors is fundamental to the life sciences, yet to date a few important pathways remain unresolved. One example is the…”
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A molecular threading mechanism underlies Jumonji lysine demethylase KDM2A regulation of methylated H3K36 by Cheng, Zhongjun, Cheung, Peggie, Kuo, Alex J, Yukl, Erik T, Wilmot, Carrie M, Gozani, Or, Patel, Dinshaw J

“…The dynamic reversible methylation of lysine residues on histone proteins is central to chromatin biology. Key components are demethylase enzymes, which remove…”
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Nuclear Magnetic Resonance Structure and Binding Studies of PqqD, a Chaperone Required in the Biosynthesis of the Bacterial Dehydrogenase Cofactor Pyrroloquinoline Quinone by Latham, John A., Xia, Youlin, Klinman, Judith P., Wilmot, Carrie M.

“…Biosynthesis of the ribosomally synthesized and post-translationally modified peptide (RiPP), pyrroloquinoline quinone (PQQ), is initiated when the precursor…”
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Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinone by Davidson, Victor L, Wilmot, Carrie M

“…Methylamine dehydrogenase (MADH) catalyzes the oxidative deamination of methylamine to formaldehyde and ammonia. Tryptophan tryptophylquinone (TTQ) is the…”
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Chlorite Dismutases, DyPs, and EfeB: 3 Microbial Heme Enzyme Families Comprise the CDE Structural Superfamily by Goblirsch, Brandon, Kurker, Richard C., Streit, Bennett R., Wilmot, Carrie M., DuBois, Jennifer L.

“…Heme proteins are extremely diverse, widespread, and versatile biocatalysts, sensors, and molecular transporters. The chlorite dismutase family of hemoproteins…”
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Larger active site in an ancestral hydroxynitrile lyase increases catalytically promiscuous esterase activity by Jones, Bryan J, Evans, 3rd, Robert L, Mylrea, Nathan J, Chaudhury, Debayan, Luo, Christine, Guan, Bo, Pierce, Colin T, Gordon, Wendy R, Wilmot, Carrie M, Kazlauskas, Romas J

“…Hydroxynitrile lyases (HNL's) belonging to the α/β-hydrolase-fold superfamily evolved from esterases approximately 100 million years ago. Reconstruction of an…”
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In Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase Complex by Jensen, Lyndal M.R, Sanishvili, Ruslan, Davidson, Victor L, Wilmot, Carrie M

“…MauG is a diheme enzyme responsible for the posttranslational modification of two tryptophan residues to form the tryptophan tryptophylquinone (TTQ) cofactor…”
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The role of protein crystallography in defining the mechanisms of biogenesis and catalysis in copper amine oxidase by Klema, Valerie J, Wilmot, Carrie M

“…Copper amine oxidases (CAOs) are a ubiquitous group of enzymes that catalyze the conversion of primary amines to aldehydes coupled to the reduction of O(2) to…”
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Mutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesis by Tarboush, Nafez Abu, Jensen, Lyndal M. R, Yukl, Erik T, Geng, Jiafeng, Liu, Aimin, Wilmot, Carrie M, Davidson, Victor L

“…The diheme enzyme MauG catalyzes the posttranslational modification of the precursor protein of methylamine dehydrogenase (preMADH) to complete biosynthesis of…”
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Diradical intermediate within the context of tryptophan tryptophylquinone biosynthesis by Yukl, Erik T., Liu, Fange, Krzystek, J., Shin, Sooim, Jensen, Lyndal M. R., Davidson, Victor L., Wilmot, Carrie M., Liu, Aimin

“…Despite the importance of tryptophan (Trp) radicals in biology, very few radicals have been trapped and characterized in a physiologically meaningful context…”
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Polysaccharide Monoxygenases: Giving a Boost to Biofuel Production by Wilmot, Carrie M.

“…In this issue of Structure, Li et al. present high resolution crystal structures of two fungal polysaccharide monoxygenases. Unexpectedly, they observe oxygen…”
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Cofactor biosynthesis through protein post-translational modification by Yukl, Erik T, Wilmot, Carrie M

“…► Maturation of metal centers with modified amino acid ligands; urease and nitrile hydratase. ► Biosynthesis of pyrroloquinoline quinone from a peptide…”
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Structural Analysis of a Ni-Methyl Species in Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis by Cedervall, Peder E, Dey, Mishtu, Li, Xianghui, Sarangi, Ritimukta, Hedman, Britt, Ragsdale, Stephen W, Wilmot, Carrie M

“…We present the 1.2 Å resolution X-ray crystal structure of a Ni-methyl species that is a proposed catalytic intermediate in methyl-coenzyme M reductase (MCR),…”
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Uncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis by Wilmot, Carrie M, Davidson, Victor L

“…Catalytic quinone cofactors derived from post-translational modification of amino acid residues within the enzyme polypeptide have roles in a variety of…”
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Exploring Molecular Oxygen Pathways in Hansenula polymorpha Copper-containing Amine Oxidase by Johnson, Bryan J., Cohen, Jordi, Welford, Richard W., Pearson, Arwen R., Schulten, Klaus, Klinman, Judith P., Wilmot, Carrie M.

“…The accessibility of large substrates to buried enzymatic active sites is dependent upon the utilization of proteinaceous channels. The necessity of these…”
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Kinetic and Structural Analysis of Substrate Specificity in Two Copper Amine Oxidases from Hansenula polymorpha by Chang, Cindy M, Klema, Valerie J, Johnson, Bryan J, Mure, Minae, Klinman, Judith P, Wilmot, Carrie M

“…The structural underpinnings of enzyme substrate specificity are investigated in a pair of copper amine oxidases (CAOs) from Hansenula polymorpha (HPAO-1 and…”
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Copper-containing amine oxidases. Biogenesis and catalysis; a structural perspective by Brazeau, Brian J., Johnson, Bryan J., Wilmot, Carrie M.

“…This review will focus on how X-ray crystallographic studies of copper-containing amine oxidases have complemented the solution, kinetic, and spectroscopic…”
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Synergy within structural biology of single crystal optical spectroscopy and X-ray crystallography by De la Mora-Rey, Teresa, Wilmot, Carrie M

“…Advances in the adaptation of optical spectroscopy to monitor photo-induced or enzyme-catalyzed reactions in the crystalline state have enabled X-ray crystal…”
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