1CEC

A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES

1CEC の概要

• エントリーDOI: 10.2210/pdb1cec/pdb
• 分子名称: ENDOGLUCANASE CELC (2 entities in total)
• 機能のキーワード: glycosyl hydrolase, cellulase, family a/5 of cellulases/glycosyl hydrolases, clostridium thermocellum, endoglucanase c, hydrolase (glycosyl)
• 由来する生物種: Clostridium thermocellum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40948.34

構造登録者

Alzari, P.M.,Dominguez, R. (登録日: 1995-06-07, 公開日: 1996-01-29, 最終更新日: 2024-02-07)

主引用文献

Dominguez, R.,Souchon, H.,Spinelli, S.,Dauter, Z.,Wilson, K.S.,Chauvaux, S.,Beguin, P.,Alzari, P.M.
A common protein fold and similar active site in two distinct families of beta-glycanases.
Nat.Struct.Biol., 2:569-576, 1995

PubMed Abstract: The structure of Clostridium thermocellum endoglucanase CelC, a member of the largest cellulase family (family A), has been determined at 2.15 A resolution. The protein folds into an (alpha/beta)8 barrel, with a deep active-site cleft generated by the insertion of a helical subdomain. The structure of the catalytic core of xylanase XynZ, which belongs to xylanase family F, has been determined at 1.4 A resolution. In spite of significant differences in substrate specificity and structure (including the absence of the helical subdomain), the general polypeptide folding pattern, architecture of the active site and catalytic mechanism of XynZ and CelC are similar, suggesting a common evolutionary origin.

PubMed: 7664125
DOI: 10.1038/nsb0795-569

実験手法

X-RAY DIFFRACTION (2.15 Å)