X-ray diffraction structure of a plant glycosyl hydrolase family 32 protein:: fructan 1-exohydrolase IIa of Cichorium intybus

被引：103

作者：

Verhaest, M

Van den Ende, W

Le Roy, K

De Ranter, CJ

Van Laere, A

Rabijns, A

机构：

[1] Katholieke Univ Leuven, Fac Farmaceut Wetenschappen, Lab Analyt Chem & Med Fysicochem, B-3000 Louvain, Belgium

[2] Katholieke Univ Leuven, Fac Wetenschappen, Dept Biol, Lab Mol Plantenfysiol, B-3001 Heverlee, Belgium

来源：

PLANT JOURNAL | 2005年 / 41卷 / 03期

关键词：

protein crystallization; X-ray crystallography; fructan degradation; fructan exohydrolase; glycosyl hydrolase family 32;

D O I：

10.1111/j.1365-313X.2004.02304.x

中图分类号：

Q94 [植物学];

学科分类号：

071001 ;

摘要：

Fructan 1-exohydrolase, an enzyme involved in fructan degradation, belongs to the glycosyl hydrolase family 32. The structure of isoenzyme 1-FEH IIa from Cichorium intybus is described at a resolution of 2.35 Angstrom. The structure consists of an N-terminal fivefold beta-propeller domain connected to two C-terminal beta-sheets. The putative active site is located entirely in the beta-propeller domain and is formed by amino acids which are highly conserved within glycosyl hydrolase family 32. The fructan-binding site is thought to be in the cleft formed between the two domains. The 1-FEH IIa structure is compared with the structures of two homologous but functionally different enzymes: a levansucrase from Bacillus subtilis (glycosyl hydrolase family 68) and an invertase from Thermotoga maritima (glycosyl hydrolase family 32).

引用

页码：400 / 411

页数：12

共 63 条

[1] The three-dimensional structure of invertase (β-fructosidase) from Thermotoga maritima reveals a bimodular arrangement and an evolutionary relationship between retaining and inverting glycosidases [J].

Alberto, F ;

Bignon, C ;

Sulzenbacher, G ;

Henrissat, B ;

Czjzek, M .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (18) :18903-18910

[2] The large subunit determines catalytic specificity of barley sucrose:fructan 6-fructosyltransferase and fescue sucrose:sucrose 1-fructosyltransferase [J].

Altenbach, D ;

Nüesch, E ;

Meyer, AD ;

Boller, T ;

Wiemken, A .

FEBS LETTERS, 2004, 567 (2-3) :214-218

[3] Substitution of Asp-309 by Asn in the Arg-Asp-Pro (RDP) motif of Acetobacter diazotrophicus levansucrase affects sucrose hydrolysis, but not enzyme specificity [J].

Batista, FR ;

Hernández, L ;

Fernández, JR ;

Arrieta, J ;

Menéndez, C ;

Gómez, R ;

Támbara, Y ;

Pons, T .

BIOCHEMICAL JOURNAL, 1999, 337 :503-506

[4] Tachylectin-2:: crystal structure of a specific GlcNAc/GalNAc-binding lectin involved in the innate immunity host defense of the Japanese horseshoe crab Tachypleus tridentatus [J].

Beisel, HG ;

Kawabata, S ;

Iwanaga, S ;

Huber, R ;

Bode, W .

EMBO JOURNAL, 1999, 18 (09) :2313-2322

[5] Crystal structure of the tricorn protease reveals a protein disassembly line [J].

Brandstetter, H ;

Kim, JS ;

Groll, M ;

Huber, R .

NATURE, 2001, 414 (6862) :466-470

[6]

Brunger AT, 1998, ACTA CRYSTALLOGR D, V54, P905, DOI 10.1107/s0907444998003254

[7] KINETIC STUDIES OF LEVANSUCRASE OF BACILLUS-SUBTILIS [J].

CHAMBERT, R ;

TREBOUL, G ;

DEDONDER, R .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1974, 41 (02) :285-300

[8] POLYMERASE AND HYDROLASE ACTIVITIES OF BACILLUS-SUBTILIS LEVANSUCRASE CAN BE SEPARATELY MODULATED BY SITE-DIRECTED MUTAGENESIS [J].

CHAMBERT, R ;

PETITGLATRON, MF .

BIOCHEMICAL JOURNAL, 1991, 279 :35-41

[9]

*COLL COMP PROJ 4, 1994, ACTA CRYSTALLOGR D, V250, P760

[10] Sialidase-like Asp-boxes: Sequence-similar structures within different protein folds [J].

Copley, RR ;

Russell, RB ;

Ponting, CP .

PROTEIN SCIENCE, 2001, 10 (02) :285-292

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