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- W4236046387 abstract "Recent crystallographic studies have revealed a range of structural changes in the three-dimensional structure of endo-1,4-xylanase (XYNII) from Trichoderma reesei. The observed conformational changes can be described as snapshots of an open-close movement of the active site of XYNII. These structures were further analyzed in this study. In addition, a total of four 1 ns molecular dynamics (MD) simulations were performed representing different states of the enzyme. A comparison of the global and local changes found in the X-ray structures and the MD runs suggested that the simulations reproduced a similar kind of active site opening and closing as predicted by the crystal structures. The open-close movement was characterized by the use of distance difference matrixes and the Hingefind program (Wriggers and Schulten, Proteins 29:1–14, 1997) to be a ‘hinge-bending’ motion involving two large rigidly-moving regions and an extended hinge. This conformational feature is probably inherent to this molecular architecture and probably plays a role in the function of XYNII. Proteins 31:434–444, 1998. © 1998 Wiley-Liss, Inc." @default.
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- W4236046387 date "1998-06-01" @default.
- W4236046387 modified "2023-09-23" @default.
- W4236046387 title "Functional conformational changes of endo‐1,4‐xylanase II from Trichoderma reesei: A molecular dynamics study" @default.
- W4236046387 doi "https://doi.org/10.1002/(sici)1097-0134(19980601)31:4<434::aid-prot9>3.3.co;2-p" @default.
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