Publication Abstract from PubMed
The 1.7A resolution crystal structure of recombinant family G/11 beta-1,4-xylanase (rXynA) from Bacillus subtilis 1A1 shows a jellyroll fold in which two curved beta-sheets form the active-site and substrate-binding cleft. The onset of thermal denaturation of rXynA occurs at 328 K, in excellent agreement with the optimum catalytic temperature. Molecular dynamics simulations at temperatures of 298-328 K demonstrate that below the optimum temperature the thumb loop and palm domain adopt a closed conformation. However, at 328 K these two domains separate facilitating substrate access to the active-site pocket, thereby accounting for the optimum catalytic temperature of the rXynA.
Correlation of temperature induced conformation change with optimum catalytic activity in the recombinant G/11 xylanase A from Bacillus subtilis strain 168 (1A1).,Murakami MT, Arni RK, Vieira DS, Degreve L, Ruller R, Ward RJ FEBS Lett. 2005 Nov 21;579(28):6505-10. Epub 2005 Nov 2. PMID:16289057[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
