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J. Biol. Chem., Vol. 280, Issue 46, 38831-38838, November 18, 2005

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Crystal Structure of Glucooligosaccharide Oxidase from Acremonium strictum

A NOVEL FLAVINYLATION OF 6-S-CYSTEINYL, 8-N1-HISTIDYL FAD^*

Chun-Hsiang Huang¶1, Wen-Lin Lai1, Meng-Hwan Lee, Chun-Jung Chen||, Andrea Vasella**, Ying-Chieh Tsai2, and Shwu-Huey Liaw¶3

From the Structural Biology Program, Institute of Biochemistry, and ^¶Faculty of Life Science, National Yang-Ming University, Taipei 11221, Taiwan, the ^||Biology Group, Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan, the ^**Laboratorium für Organische Chemie, ETH Hönggerberg, CH-8093 Zürich, Switzerland, and the Department of Medical Research and Education, Taipei Veterans General Hospital, Taipei 11217, Taiwan

Glucooligosaccharide oxidase from Acremonium strictum has been screened for potential applications in oligosaccharide acid production and alternative carbohydrate detection, because it catalyzes the oxidation of glucose, maltose, lactose, cellobiose and cello- and maltooligosaccharides. We report the crystal structures of the enzyme and of its complex with an inhibitor, 5-amino-5-deoxy- cellobiono-1,5-lactam at 1.55- and 1.98-Å resolution, respectively. Unexpectedly, the protein structure demonstrates the first known double attachment flavinylation, 6-S-cysteinyl, 8-N1-histidyl FAD. The FAD cofactor is cross-linked to the enzyme via the C⁶ atom and the 8-methyl group of the isoalloxazine ring with Cys¹³⁰ and His⁷⁰, respectively. This sugar oxidase possesses an open carbohydrate-binding groove, allowing the accommodation of higher oligosaccharides. The complex structure suggests that this enzyme may prefer a -D-glucosyl residue at the reducing end with the conserved Tyr⁴²⁹ acting as a general base to abstract the OH¹ proton in concert with the H¹ hydride transfer to the flavin N⁵. Finally, a detailed comparison illustrates the structural conservation as well as the divergence between this protein and its related flavoenzymes.

Received for publication, June 3, 2005 , and in revised form, September 7, 2005.

The atomic coordinates and structure factors (codes 1ZR6 and 2AXR) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by the National Science Council (NSC93-2311-B010-009). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Both authors contributed equally to this work.

² To whom correspondence may be addressed: Institute of Biochemistry, National Yang-Ming University, Taipei 11221, Taiwan. Tel.: 886-2-2826-7125; Fax: 886-2826-4843; E-mail: tasiyc{at}edu.tw.

³ To whom correspondence may be addressed: Faculty of Life Science, National Yang-Ming University, Taipei 11221, Taiwan. Tel.: 886-2-2826-7278; Fax: 886-2-2820-2449; E-mail: shliaw{at}ym.edu.tw.

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