This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1ob0
From Proteopedia
(Difference between revisions)
m (Protected "1ob0" [edit=sysop:move=sysop]) |
Revision as of 19:41, 14 March 2011
KINETIC STABILIZATION OF BACILLUS LICHENIFORMIS-AMYLASE THROUGH INTRODUCTION OF HYDROPHOBIC RESIDUES AT THE SURFACE
Template:ABSTRACT PUBMED 12540849
About this Structure
1ob0 is a 1 chain structure with sequence from Bacillus licheniformis. Full crystallographic information is available from OCA.
Reference
- Machius M, Declerck N, Huber R, Wiegand G. Kinetic stabilization of Bacillus licheniformis alpha-amylase through introduction of hydrophobic residues at the surface. J Biol Chem. 2003 Mar 28;278(13):11546-53. Epub 2003 Jan 21. PMID:12540849 doi:10.1074/jbc.M212618200
- Hwang KY, Song HK, Chang C, Lee J, Lee SY, Kim KK, Choe S, Sweet RM, Suh SW. Crystal structure of thermostable alpha-amylase from Bacillus licheniformis refined at 1.7 A resolution. Mol Cells. 1997 Apr 30;7(2):251-8. PMID:9163741
- Machius M, Declerck N, Huber R, Wiegand G. Activation of Bacillus licheniformis alpha-amylase through a disorder-->order transition of the substrate-binding site mediated by a calcium-sodium-calcium metal triad. Structure. 1998 Mar 15;6(3):281-92. PMID:9551551
- Machius M, Wiegand G, Huber R. Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase at 2.2 A resolution. J Mol Biol. 1995 Mar 3;246(4):545-59. PMID:7877175 doi:http://dx.doi.org/10.1006/jmbi.1994.0106
