1XAS

CRYSTAL STRUCTURE, AT 2.6 ANGSTROMS RESOLUTION, OF THE STREPTOMYCES LIVIDANS XYLANASE A, A MEMBER OF THE F FAMILY OF BETA-1,4-D-GLYCANSES

Summary for 1XAS

• Entry DOI: 10.2210/pdb1xas/pdb
• Descriptor: 1,4-BETA-D-XYLAN XYLANOHYDROLASE (1 entity in total)
• Functional Keywords: xylanase a
• Biological source: Streptomyces lividans
• Total number of polymer chains: 1
• Total formula weight: 32971.39

Authors

Derewenda, U.,Derewenda, Z.S. (deposition date: 1994-05-31, release date: 1995-05-31, Last modification date: 2024-02-14)

Primary citation

Derewenda, U.,Swenson, L.,Green, R.,Wei, Y.,Morosoli, R.,Shareck, F.,Kluepfel, D.,Derewenda, Z.S.
Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases.
J.Biol.Chem., 269:20811-20814, 1994

PubMed Abstract: The crystal structure of the 32-kDa catalytic domain of the Streptomyces lividans xylanase A was solved by molecular isomorphous replacement methods and subsequently refined at 2.6-A resolution to a conventional crystallographic R factor of 0.21. This is the first successful structure determination of a member of the F family of endo-beta-1,4-D-glycanases. Unlike the recently determined xylanases of the G family (Wakarchuk, W. W., Campbell, R. L., Sung, W. L., Davoodi, J., and Yaguchi, M. (1994) Protein Sci. 3, 467-475), where the catalytic domains have a unique beta-sheet structure, the 32-kDa domain of the S. lividans xylanase A is folded into a complete (alpha/beta)8 barrel, the first such fold observed among beta-1,4-D-glycanases. The active site is located at the carbonyl end of the beta barrel. The crystal structure supports the earlier assignment of Glu-128 and Glu-236 as the catalytic amino acids (Moreau, A., Roberge, M., Manin, C., Shareck, F., Kluepfel, D., and Morosoli, R. (1994) Biochem. J., in press).

PubMed: 8063693

Experimental method

X-RAY DIFFRACTION (2.6 Å)