CRYSTAL AND MOLECULAR-STRUCTURE AT 0.16-NM RESOLUTION OF THE HYBRID BACILLUS ENDO-1,3-1,4-BETA-D-GLUCAN 4-GLUCANOHYDROLASE H(A16-M)

被引:25
作者
HAHN, M
KEITEL, T
HEINEMANN, U
机构
[1] MAX DELBRUCK CENTRUM MOLEK MED,KRISTALLOG FORSCHUNGSGRP,D-13122 BERLIN,GERMANY
[2] FREE UNIV BERLIN,INST KRISTALLOG,W-1000 BERLIN,GERMANY
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1995年 / 232卷 / 03期
关键词
PROTEIN STRUCTURE; X-RAY CRYSTALLOGRAPHY; 1,3-1,4-BETA-GLUCANASE; BETA-GLUCAN HYDROLYSIS; SUBSTRATE SPECIFICITY;
D O I
10.1111/j.1432-1033.1995.849zz.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
H(A16-M) is a hybrid endo-1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus. Its crystal structure was refined using synchrotron X-ray diffraction data up to a maximal resolution of 0.16 nm. The R value of the resulting model is 14.3% against 21 032 reflections > 2 sigma. 93% of the amino acid residues are in the most favorable regions of the Ramachandran diagram, and geometrical parameters are in accordance with other proteins solved at high resolution. As shown earlier [Keitel, T., Simon, O., Borriss, R. & Heinemann, U. (1993) Proc. Natl Acad. Sci. USA 90, 5287-5291], the protein folds into a compact jellyroll-type beta-sheet structure. A systematic analysis of the secondary structure reveals the presence of two major antiparallel beta-sheets and a three-stranded minor mixed sheet. Amino acid residues involved in catalysis and substrate binding are located inside a deep channel spanning the surface of the protein. To investigate the stereochemical cause of the observed specificity of endo-1,3-1,4-beta-D-glucan 4-glucanohydrolases towards beta-1,4 glycosyl bonds adjacent to beta-1,3 bonds, the high-resolution crystal structure has been used to model an enzyme-substrate complex. It is proposed that productive substrate binding to the subsites p1, p2 and p3 of H(A16-M) requires a beta-1,3 linkage between glucose units bound to p1 and p2.
引用
收藏
页码:849 / 858
页数:10
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