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Crystal structure and carbohydrate-binding properties of the human cartilage glycoprotein-39

Autor: Fusetti, F, Pijning, T, Kalk, KH, Bos, E, Dijkstra, BW, Dijkstra, Bauke W.

Publikováno v: The Journal of Biological Chemistry, 278(39), 37753-37760. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

The human cartilage glycoprotein-39 (HCgp-39 or YKL40) is expressed by synovial cells and macrophages during inflammation. Its precise physiological role is unknown. However, it has been proposed that HCgp-39 acts as an autoantigen in rheumatoid arth

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a903273db7aef9ad1a5fce4af0c5716
https://pubmed.ncbi.nlm.nih.gov/12851408

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Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni - Structural basis for substrate oxidation and electron transfer

Autor: Oubrie, A, Rozeboom, HJ, Kalk, KH, Huizinga, EG, Dijkstra, BW, Huizinga, Eric G., Dijkstra, Bauke W.

Publikováno v: The Journal of Biological Chemistry, 277(5), 3727-3732. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Quinoprotein alcohol dehydrogenases are redox enzymes that participate in distinctive catabolic pathways that enable bacteria to grow on various alcohols as the sole source of carbon and energy. The x-ray structure of the quinohemoprotein alcohol deh

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::8c45c811ede6a319a60d194509b83a4e
https://research.rug.nl/en/publications/cc9b0b3b-47ac-480a-ba37-9bb27bd364c3

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The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-angstrom resolution

Autor: Uitdehaag, JCM, Kalk, KH, Dijkhuizen, L, Dijkstra, BW

Publikováno v: The Journal of Biological Chemistry, 274(49), 34868-34876. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

The enzyme cyclodextrin glycosyltransferase is closely related to alpha-amylases but has the unique ability to produce cyclodextrins (circular alpha(1-->4)-linked glucoses) from starch. To characterize this specificity we determined a 1.8-Angstrom st

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::e04a0334ffb278fadfb9bfda271a4a74
https://research.rug.nl/en/publications/d4b4b5a0-5f36-4cc1-9282-3d25cd785153

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1.68-angstrom crystal structure of endopolygalacturonase II from Aspergillus niger and identification of active site residues by site-directed mutagenesis

Autor: van Santen, Y, Benen, JAE, Schroter, KH, Kalk, KH, Armand, S, Visser, J., Dijkstra, BW

Publikováno v: The Journal of Biological Chemistry, 274(43), 30474-30480. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Polygalacturonases specifically hydrolyze polygalaturonate, a major constituent of plant cell wall pectin. To understand the catalytic mechanism and substrate and product specificity of these enzymes, we have solved the x-ray structure of endopolygal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::e739623461df71cca27114ec3f14c1f0
https://research.rug.nl/en/publications/596ce865-a371-47df-b264-61ad1a77dc16

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The 1.7 angstrom crystal structure of the apo form of the soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus reveals a novel internal conserved sequence repeat

Autor: Oubrie, A, Rozeboom, HJ, Kalk, KH, Duine, JA, Dijkstra, BW

Publikováno v: Journal of Molecular Biology, 289(2), 319-333. Academic Press

The crystal structure of a dimeric apo form of the soluble quinoprotein glucose dehydrogenase (s-GDH) from Acinetobacter calcoaceticus has been solved by multiple isomorphous replacement followed by density modification, and was subsequently refined

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::b8929d47bd1a460b3fc385d33cd2c2cc
https://research.rug.nl/en/publications/6dc95f96-681d-4053-9b37-2524f71b2202

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The X-ray Structure of Epoxide Hydrolase from Agrobacterium radiobacter AD1. An Enzyme to Detoxify Harmful Epoxides

Autor: Nardini, M, Ridder, IS, Rozeboom, HJ, Kalk, KH, Rink, R, Janssen, DB, Dijkstra, BW

Publikováno v: The Journal of Biological Chemistry, 274(21), 14579-14586. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Epoxide hydrolases catalyze the cofactor-independent hydrolysis of reactive and toxic epoxides, They play an essential role in the detoxification of various xenobiotics in higher organisms and in the bacterial degradation of several environmental pol

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::14c4a4e7af7a269d1a6f08c8259fa9f0
https://research.rug.nl/en/publications/1686e182-dada-429c-9bd2-575679b0529f

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X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family

Autor: Uitdehaag, JCM, Mosi, R, Kalk, KH, Dijkhuizen, L, Withers, SG, Dijkstra, BW

Publikováno v: Nature Structural Biology, 6(5), 432-436

Cyclodextrin glycosyltransferase (CGTase) is an enzyme of the alpha-amylase family, which uses a double displacement mechanism to process alpha-linked glucose polymers. We have determined two X-ray structures of CGTase complexes, one with an intact s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::d41a5c7084fabf78d710ff67e0b2f689
https://research.rug.nl/en/publications/f95e3cae-fdaf-4322-b355-8eaf1e075070

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Crystal structure of a murine alpha-class glutathione S-transferase involved in cellular defense against oxidative stress

Autor: Krengel, U, Schroter, KH, Hoier, H, Arkema, A, Kalk, KH, Zimniak, P, Dijkstra, BW

Publikováno v: FEBS Letters, 422(3), 285-290. Wiley

Glutathione S-transferases (GSTs) are ubiquitous multifunctional enzymes which play a key role in cellular detoxification, The enzymes protect the cells against toxicants by conjugating them to glutathione, Recently, a novel subgroup of alpha-class G

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::4022c2a498af77eb02ba5c34e62a2b62
https://research.rug.nl/en/publications/30a5606c-6513-433b-afb6-15c8bc4c8266

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X-ray structure of antistasin at 1.9 angstrom resolution and its modelled complex with blood coagulation factor Xa

Autor: Lapatto, R, Krengel, U, Schreuder, HA, Arkema, A, deBoer, B, Kalk, KH, Hol, WGJ, Grootenhuis, PDJ, Mulders, JWM, Dijkema, R, Theunissen, HJM, Dijkstra, BW

Publikováno v: EMBO Journal, 16(17), 5151-5161. Wiley

The three-dimensional structure of antistasin, a potent inhibitor of blood coagulation factor Xa, from the Mexican leech Haementeria officinalis was determined at 1.9 Angstrom resolution by X-ray crystallography, The structure reveals a novel protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::4b1c9879a23122108ade89c814799203
https://research.rug.nl/en/publications/a0ff9b7a-f1c8-412b-a01c-295e7df43662

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