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Biosynthesis of a 3,6-dideoxyhexose: crystallization and X-ray diffraction of CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1) for ascarylose biosynthesis.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 01; 62(Pt 3):231-4.AC

Abstract

CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1), along with its reductase (E3), catalyzes the unusual C-3 deoxygenation of CDP-6-deoxy-L-threo-D-glycero-4-hexulose to form CDP-3,6-dideoxy-L-threo-D-glycero-4-hexulose in CDP-ascarylose biosynthesis [Chen et al. (1996), Biochemistry, 35, 16412-16420]. This dimeric [2Fe-2S] protein, cloned from the bacteria Yersinia pseudotuberculosis, is currently the only known example of an enzyme that uses a vitamin B6-derived pyridoxamine 5'-phosphate (PMP) cofactor to carry out one-electron chemistry [Agnihotri & Liu (2001), Bioorg. Chem. 29, 234-257]. It also exhibits a [2Fe-2S] cluster-binding motif (C-X57-C-X1-C-X7-C) which has not been observed previously [Agnihotri et al. (2004), Biochemistry, 43, 14265-14274] The recombinant 97.7 kDa dimer was crystallized in the trigonal space group P3(2), with unit-cell parameters a = b = 97.37, c = 142.2 A, alpha = beta = 90, gamma = 120 degrees. A data set has been collected to 1.9 A resolution. A full MAD data set was also collected at the iron absorption edge that diffracted to 2.0 A.

Authors+Show Affiliations

Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural

Language

eng

PubMed ID

16511309

Citation

Smith, Peter, et al. "Biosynthesis of a 3,6-dideoxyhexose: Crystallization and X-ray Diffraction of CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1) for Ascarylose Biosynthesis." Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 62, no. Pt 3, 2006, pp. 231-4.
Smith P, Lin A, Szu PH, et al. Biosynthesis of a 3,6-dideoxyhexose: crystallization and X-ray diffraction of CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1) for ascarylose biosynthesis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006;62(Pt 3):231-4.
Smith, P., Lin, A., Szu, P. H., Liu, H. W., & Tsai, S. C. (2006). Biosynthesis of a 3,6-dideoxyhexose: crystallization and X-ray diffraction of CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1) for ascarylose biosynthesis. Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 62(Pt 3), 231-4.
Smith P, et al. Biosynthesis of a 3,6-dideoxyhexose: Crystallization and X-ray Diffraction of CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1) for Ascarylose Biosynthesis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Mar 1;62(Pt 3):231-4. PubMed PMID: 16511309.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Biosynthesis of a 3,6-dideoxyhexose: crystallization and X-ray diffraction of CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1) for ascarylose biosynthesis. AU - Smith,Peter, AU - Lin,Ava, AU - Szu,Pin-hui, AU - Liu,Hung-wen, AU - Tsai,Shiou-Chuan, Y1 - 2006/02/10/ PY - 2005/11/22/received PY - 2006/01/30/accepted PY - 2006/3/3/pubmed PY - 2006/4/14/medline PY - 2006/3/3/entrez SP - 231 EP - 4 JF - Acta crystallographica. Section F, Structural biology and crystallization communications JO - Acta Crystallogr Sect F Struct Biol Cryst Commun VL - 62 IS - Pt 3 N2 - CDP-6-deoxy-L-threo-D-glycero-4-hexulose-3-dehydrase (E1), along with its reductase (E3), catalyzes the unusual C-3 deoxygenation of CDP-6-deoxy-L-threo-D-glycero-4-hexulose to form CDP-3,6-dideoxy-L-threo-D-glycero-4-hexulose in CDP-ascarylose biosynthesis [Chen et al. (1996), Biochemistry, 35, 16412-16420]. This dimeric [2Fe-2S] protein, cloned from the bacteria Yersinia pseudotuberculosis, is currently the only known example of an enzyme that uses a vitamin B6-derived pyridoxamine 5'-phosphate (PMP) cofactor to carry out one-electron chemistry [Agnihotri & Liu (2001), Bioorg. Chem. 29, 234-257]. It also exhibits a [2Fe-2S] cluster-binding motif (C-X57-C-X1-C-X7-C) which has not been observed previously [Agnihotri et al. (2004), Biochemistry, 43, 14265-14274] The recombinant 97.7 kDa dimer was crystallized in the trigonal space group P3(2), with unit-cell parameters a = b = 97.37, c = 142.2 A, alpha = beta = 90, gamma = 120 degrees. A data set has been collected to 1.9 A resolution. A full MAD data set was also collected at the iron absorption edge that diffracted to 2.0 A. SN - 1744-3091 UR - https://www.unboundmedicine.com/medline/citation/16511309/Biosynthesis_of_a_36_dideoxyhexose:_crystallization_and_X_ray_diffraction_of_CDP_6_deoxy_L_threo_D_glycero_4_hexulose_3_dehydrase__E1__for_ascarylose_biosynthesis_ L2 - http://scripts.iucr.org/cgi-bin/paper?S1744309106003721 DB - PRIME DP - Unbound Medicine ER -