1V6Y

Crystal Structure Of chimeric Xylanase between Streptomyces Olivaceoviridis E-86 FXYN and Cellulomonas fimi Cex

Summary for 1V6Y

• Entry DOI: 10.2210/pdb1v6y/pdb
• Related: 1xyf 2exo
• Descriptor: Beta-xylanase,Exoglucanase/xylanase (2 entities in total)
• Functional Keywords: xylanase, tim-barrel, chimeric enzyme, hydrolase
• Biological source: Streptomyces olivaceoviridis; More
• Total number of polymer chains: 1
• Total formula weight: 35972.09

Authors

Kaneko, S.,Ichinose, H.,Fujimoto, Z.,Kuno, A.,Yura, K.,Go, M.,Mizuno, H.,Kusakabe, I.,Kobayashi, H. (deposition date: 2003-12-04, release date: 2004-09-07, Last modification date: 2024-04-10)

Primary citation

Kaneko, S.,Ichinose, H.,Fujimoto, Z.,Kuno, A.,Yura, K.,Go, M.,Mizuno, H.,Kusakabe, I.,Kobayashi, H.
Structure and function of a family 10 beta-xylanase chimera of Streptomyces olivaceoviridis E-86 FXYN and Cellulomonas fimi Cex
J.Biol.Chem., 279:26619-26626, 2004

PubMed Abstract: The catalytic domain of xylanases belonging to glycoside hydrolase family 10 (GH10) can be divided into 22 modules (M1 to M22; Sato, Y., Niimura, Y., Yura, K., and Go, M. (1999) Gene (Amst.) 238, 93-101). Inspection of the crystal structure of a GH10 xylanase from Streptomyces olivaceoviridis E-86 (SoXyn10A) revealed that the catalytic domain of GH10 xylanases can be dissected into two parts, an N-terminal larger region and C-terminal smaller region, by the substrate binding cleft, corresponding to the module border between M14 and M15. It has been suggested that the topology of the substrate binding clefts of GH10 xylanases are not conserved (Charnock, S. J., Spurway, T. D., Xie, H., Beylot, M. H., Virden, R., Warren, R. A. J., Hazlewood, G. P., and Gilbert, H. J. (1998) J. Biol. Chem. 273, 32187-32199). To facilitate a greater understanding of the structure-function relationship of the substrate binding cleft of GH10 xylanases, a chimeric xylanase between SoXyn10A and Xyn10A from Cellulomonas fimi (CfXyn10A) was constructed, and the topology of the hybrid substrate binding cleft established. At the three-dimensional level, SoXyn10A and CfXyn10A appear to possess 5 subsites, with the amino acid residues comprising subsites -3 to +1 being well conserved, although the +2 subsites are quite different. Biochemical analyses of the chimeric enzyme along with SoXyn10A and CfXyn10A indicated that differences in the structure of subsite +2 influence bond cleavage frequencies and the catalytic efficiency of xylooligosaccharide hydrolysis. The hybrid enzyme constructed in this study displays fascinating biochemistry, with an interesting combination of properties from the parent enzymes, resulting in a low production of xylose.

PubMed: 15078885
DOI: 10.1074/jbc.M308899200

Experimental method

X-RAY DIFFRACTION (2.2 Å)