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

[41] Processing of X-ray diffraction data collected in oscillation mode [J].

Otwinowski, Z ;

Minor, W .

MACROMOLECULAR CRYSTALLOGRAPHY, PT A, 1997, 276 :307-326

[42] Transgenic tobacco plants accumulating osmolytes show reduced oxidative damage under freezing stress [J].

Parvanova, D ;

Ivanov, S ;

Konstantinova, T ;

Karanov, E ;

Atanassov, A ;

Tsvetkov, T ;

Alexieva, V ;

Djilianov, D .

PLANT PHYSIOLOGY AND BIOCHEMISTRY, 2004, 42 (01) :57-63

[43] Automated protein model building combined with iterative structure refinement [J].

Perrakis, A ;

Morris, R ;

Lamzin, VS .

NATURE STRUCTURAL BIOLOGY, 1999, 6 (05) :458-463

[44] Prediction of a common β-propeller catalytic domain for fructosyltransferases of different origin and substrate specificity [J].

Pons, T ;

Hernández, L ;

Batista, FR ;

Chinea, G .

PROTEIN SCIENCE, 2000, 9 (11) :2285-2291

[45] Studies on identifying the catalytic role of Glu-204 in the active site of yeast invertase [J].

Reddy, A ;

Maley, F .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (24) :13953-13958

[46]

REDDY VA, 1990, J BIOL CHEM, V265, P10817

[47] Fructans: beneficial for plants and humans [J].

Ritsema, T ;

Smeekens, S .

CURRENT OPINION IN PLANT BIOLOGY, 2003, 6 (03) :223-230

[48] Dietary fructans [J].

Roberfroid, MB ;

Delzenne, NM .

ANNUAL REVIEW OF NUTRITION, 1998, 18 :117-143

[49] Unexpected presence of fructan 6-exohydrolases (6-FEHs) in non-fructan plants:: characterization, cloning, mass mapping and functional analysis of a novel 'cell-wall invertase-like' specific 6-FEH from sugar beet (Beta vulgaris L.) [J].

Van den Ende, W ;

De Coninck, B ;

Clerens, S ;

Vergauwen, R ;

Van Laere, A .

PLANT JOURNAL, 2003, 36 (05) :697-710

[50] Defoliation induces fructan 1-exohydrolase II in witloof chicory roots. Cloning and purification of two isoforms, fructan 1-exohydrolase IIa and fructan 1-exohydrolase IIb. Mass fingerprint of the fructan 1-exohydrolase II enzymes [J].

Van den Ende, W ;

Michiels, A ;

Van Wonterghem, D ;

Clerens, SP ;

De Roover, J ;

Van Laere, AJ .

PLANT PHYSIOLOGY, 2001, 126 (03) :1186-1195

← 1 2 3 4 5 6 7 →