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Trypanosoma brucei UDP-galactose-4'-epimerase in ternary complex with NAD+ and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose

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Published

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Trypanosoma brucei UDP-galactose-4'-epimerase in ternary complex with NAD+ and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose. / Alphey, Magnus S.; Burton, Andrew; Urbaniak, Michael D. et al.
In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Vol. 62, No. 9, 01.09.2006, p. 829-834.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

Alphey, MS, Burton, A, Urbaniak, MD, Boons, G-J, Ferguson, MAJ & Hunter, WN 2006, 'Trypanosoma brucei UDP-galactose-4'-epimerase in ternary complex with NAD+ and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 62, no. 9, pp. 829-834. https://doi.org/10.1107/S1744309106028740

APA

Alphey, M. S., Burton, A., Urbaniak, M. D., Boons, G-J., Ferguson, M. A. J., & Hunter, W. N. (2006). Trypanosoma brucei UDP-galactose-4'-epimerase in ternary complex with NAD+ and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 62(9), 829-834. https://doi.org/10.1107/S1744309106028740

Vancouver

Alphey MS, Burton A, Urbaniak MD, Boons G-J, Ferguson MAJ, Hunter WN. Trypanosoma brucei UDP-galactose-4'-epimerase in ternary complex with NAD+ and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose. Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2006 Sept 1;62(9):829-834. doi: 10.1107/S1744309106028740

Author

Alphey, Magnus S. ; Burton, Andrew ; Urbaniak, Michael D. et al. / Trypanosoma brucei UDP-galactose-4'-epimerase in ternary complex with NAD+ and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose. In: Acta Crystallographica Section F: Structural Biology and Crystallization Communications. 2006 ; Vol. 62, No. 9. pp. 829-834.

Bibtex

@article{081625a3e5be4ccd87f4dd2efecc4f8e,
title = "Trypanosoma brucei UDP-galactose-4'-epimerase in ternary complex with NAD+ and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose",
abstract = "The structure of the NAD-dependent oxidoreductase UDP-galactose-4'-epimerase from Trypanosoma brucei in complex with cofactor and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose has been determined using diffraction data to 2.7 A resolution. Despite the high level of sequence and structure conservation between the trypanosomatid enzyme and those from humans, yeast and bacteria, the binding of the 4-fluoro-alpha-D-galactose moiety is distinct from previously reported structures. Of particular note is the observation that when bound to the T. brucei enzyme, the galactose moiety of this fluoro-derivative is rotated approximately 180 degrees with respect to the orientation of the hexose component of UDP-glucose when in complex with the human enzyme. The architecture of the catalytic centre is designed to effectively bind different orientations of the hexose, a finding that is consistent with a mechanism that requires the sugar to maintain a degree of flexibility within the active site.",
keywords = "Animals, Catalytic Domain, Crystallography, X-Ray, NAD, Protein Structure, Secondary, Substrate Specificity, Trypanosoma brucei brucei, UDPglucose 4-Epimerase, Uridine Diphosphate Galactose",
author = "Alphey, {Magnus S.} and Andrew Burton and Urbaniak, {Michael D.} and Geert-Jan Boons and Ferguson, {Michael A. J.} and Hunter, {William N.}",
year = "2006",
month = sep,
day = "1",
doi = "10.1107/S1744309106028740",
language = "English",
volume = "62",
pages = "829--834",
journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",
publisher = "Wiley-Blackwell",
number = "9",

}

RIS

TY - JOUR

T1 - Trypanosoma brucei UDP-galactose-4'-epimerase in ternary complex with NAD+ and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose

AU - Alphey, Magnus S.

AU - Burton, Andrew

AU - Urbaniak, Michael D.

AU - Boons, Geert-Jan

AU - Ferguson, Michael A. J.

AU - Hunter, William N.

PY - 2006/9/1

Y1 - 2006/9/1

N2 - The structure of the NAD-dependent oxidoreductase UDP-galactose-4'-epimerase from Trypanosoma brucei in complex with cofactor and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose has been determined using diffraction data to 2.7 A resolution. Despite the high level of sequence and structure conservation between the trypanosomatid enzyme and those from humans, yeast and bacteria, the binding of the 4-fluoro-alpha-D-galactose moiety is distinct from previously reported structures. Of particular note is the observation that when bound to the T. brucei enzyme, the galactose moiety of this fluoro-derivative is rotated approximately 180 degrees with respect to the orientation of the hexose component of UDP-glucose when in complex with the human enzyme. The architecture of the catalytic centre is designed to effectively bind different orientations of the hexose, a finding that is consistent with a mechanism that requires the sugar to maintain a degree of flexibility within the active site.

AB - The structure of the NAD-dependent oxidoreductase UDP-galactose-4'-epimerase from Trypanosoma brucei in complex with cofactor and the substrate analogue UDP-4-deoxy-4-fluoro-alpha-D-galactose has been determined using diffraction data to 2.7 A resolution. Despite the high level of sequence and structure conservation between the trypanosomatid enzyme and those from humans, yeast and bacteria, the binding of the 4-fluoro-alpha-D-galactose moiety is distinct from previously reported structures. Of particular note is the observation that when bound to the T. brucei enzyme, the galactose moiety of this fluoro-derivative is rotated approximately 180 degrees with respect to the orientation of the hexose component of UDP-glucose when in complex with the human enzyme. The architecture of the catalytic centre is designed to effectively bind different orientations of the hexose, a finding that is consistent with a mechanism that requires the sugar to maintain a degree of flexibility within the active site.

KW - Animals

KW - Catalytic Domain

KW - Crystallography, X-Ray

KW - NAD

KW - Protein Structure, Secondary

KW - Substrate Specificity

KW - Trypanosoma brucei brucei

KW - UDPglucose 4-Epimerase

KW - Uridine Diphosphate Galactose

U2 - 10.1107/S1744309106028740

DO - 10.1107/S1744309106028740

M3 - Journal article

C2 - 16946458

VL - 62

SP - 829

EP - 834

JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 9

ER -