Hahn M, Pons J, Planas A, Querol E, Heinemann U
Forschungsgruppe Kristallographie, Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany.
FEBS Lett. 1995 Oct 30;374(2):221-4. doi: 10.1016/0014-5793(95)01111-q.
The crystal structure of the 1,3-1,4-beta-D-glucan 4-glucanohydrolase from Bacillus licheniformis is solved at a resolution of 1.8 A and refined to R = 16.5%. The protein has a similar beta-sandwich structure as the homologous enzyme from Bacillus macerans and the hybrid H(A16-M). This demonstrates that the jellyroll fold of these proteins is remarkably rigid and only weakly influenced by crystal contacts. The crystal structure permits to extend mechanistic considerations derived for the B. licheniformis enzyme to the entire class of bacterial 1,3-1,4-beta-D-glucan 4-glucanohydrolases.
地衣芽孢杆菌1,3 - 1,4-β-D-葡聚糖4-葡聚糖水解酶的晶体结构在1.8 Å分辨率下解析完成,并精修至R = 16.5%。该蛋白质具有与来自浸麻芽孢杆菌的同源酶以及杂交体H(A16 - M)相似的β-三明治结构。这表明这些蛋白质的果冻卷折叠结构非常刚性,仅受晶体接触的微弱影响。晶体结构使得从地衣芽孢杆菌酶推导得出的机制考量能够扩展至整个细菌1,3 - 1,4-β-D-葡聚糖4-葡聚糖水解酶类别。