1IGO

Family 11 xylanase

Summary for 1IGO

• Entry DOI: 10.2210/pdb1igo/pdb
• Descriptor: family 11 xylanase, SULFATE ION (3 entities in total)
• Functional Keywords: xylanase, endo-1, 4-beta xylanase, family 11 xylanase, family g xylanase, hydrolase
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 45261.94

Authors

Oakley, A.J.,Thomson, C.,Heinrich, T.,Dunlop, R.,Wilce, M.C.J. (deposition date: 2001-04-18, release date: 2002-04-18, Last modification date: 2023-08-16)

Primary citation

Oakley, A.J.,Heinrich, T.,Thompson, C.A.,Wilce, M.C.
Characterization of a family 11 xylanase from Bacillus subtillis B230 used for paper bleaching.
Acta Crystallogr.,Sect.D, 59:627-636, 2003

PubMed Abstract: Enzymes such as family 11 xylanases are increasingly being used for industrial applications. Here, the cloning, structure determination and temperature-stability data of a family 11 xylanase, Xyn11X, from the alkali-tolerant Bacillus subtilis subspecies B230 are reported. This enzyme, which degrades xylan polymers, is being produced on an industrial scale for use in the paper-bleaching industry. Xyn11X adopts the canonical family 11 xylanase fold. It has a greater abundance of side chain to side chain hydrogen bonds compared with all other family 11 xylanase crystal structures. Means by which the thermostability of Xyn11X might be improved are suggested.

PubMed: 12657781
DOI: 10.1107/S0907444903001227

Experimental method

X-RAY DIFFRACTION (2.2 Å)