Structural characterization of the bifunctional glucanase-xylanase CelM2 reveals the metal effect and substrate-binding moiety

Ki Hyun Nam, Won Ho Lee, Kyung Hee Rhee, Kwang Yeon Hwang

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


The bifunctional glycoside hydrolase enzyme, CelM2, is able to hydrolyze glucan and xylan effectively. The crystal structure of this protein has been determined, providing useful sequential and structural information [K.H. Nam, S.J. Kim, K.Y. Hwang, Crystal structure of CelM2, a bifunctional glucanase-xylanase protein from a metagenome library, Biochem. Biophys. Res. Commun. 383 (2009) 183-186]. In addition, this protein is a good model for understanding bifunctional enzymes, and it will provide information relevant for genetic engineering that will be useful in the design of bifunctional proteins. However, previous structural characterization was not sufficient to develop an understanding of the metal ion and substrate-binding moiety. Herein, we determined the metal-binding site of CelM2 using zinc ions. Our results revealed that the zinc ions participate in the crystallographic packing and enzyme folding of the external region of the TIM-like barrel domain. Based on our structure, zinc ions induce the passive form of the CAP region at the catalytic cleft of the CelM2 protein. Moreover, glucose was bound to the CelM2 structure at the catalytic site. This structure provides the binding moiety that binds to the hydroxyl group of substrates such as cellulose. In addition, a structural comparison of celM2 with Cel44 provides a good model of the binding mode of CelM2. Thus, our study represents a novel structural characterization of the metal-binding site and the structure of the complex formed between CelM2 and its substrate.

Original languageEnglish
Pages (from-to)1726-1730
Number of pages5
JournalBiochemical and biophysical research communications
Issue number4
Publication statusPublished - 2010 Jan 22

Bibliographical note

Funding Information:
We thank the staff at Beamline 4A of the Pohang Light Source Korea for their assistance with the data collection. This work was supported by financial support from the Korea Institute of Environmental Science and Technology (Grant No. 2009-02001-0062-0 ). K.H. Nam is supported by the BK21 program.


  • CelM2
  • Glucanase-xylanase
  • Molecular modeling
  • Substrate-binding moiety
  • Zinc-ion binding

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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