This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1xas
From Proteopedia
|
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
Overview
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).
About this Structure
1XAS is a Single protein structure of sequence from Streptomyces lividans. Active as Endo-1,4-beta-xylanase, with EC number 3.2.1.8 Full crystallographic information is available from OCA.
Reference
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., Derewenda U, Swenson L, Green R, Wei Y, Morosoli R, Shareck F, Kluepfel D, Derewenda ZS, J Biol Chem. 1994 Aug 19;269(33):20811-4. PMID:8063693
Page seeded by OCA on Wed Nov 21 05:57:00 2007
