Crystal stuctures of MglB-2 (TP0684), a topologically variant d-glucose-binding protein from Treponema pallidum, reveal a ligand-induced conformational change: Conformational Changes in TpMglB-2
- Department of Biophysics, The University of Texas Southwestern Medical Center, Dallas Texas 75390; Department of Microbiology, The University of Texas Southwestern Medical Center, Dallas Texas 75390
- Department of Microbiology, The University of Texas Southwestern Medical Center, Dallas Texas 75390
- Research Organization:
- Argonne National Laboratory (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Organization:
- DOE - BASIC ENERGY SCIENCES
- OSTI ID:
- 1435827
- Journal Information:
- Protein Science, Vol. 27, Issue 4; ISSN 0961-8368
- Publisher:
- The Protein Society
- Country of Publication:
- United States
- Language:
- ENGLISH
Similar Records
The Tp0684 (MglB-2) Lipoprotein of Treponema pallidum: A Glucose-Binding Protein with Divergent Topology
The Tp0684 (MglB-2) Lipoprotein of Treponema pallidum: A Glucose-Binding Protein with Divergent Topo
The Tp0684 (MglB-2) Lipoprotein of Treponema pallidum: A Glucose-Binding Protein with Divergent Topo
Journal Article
·
Thu Aug 18 00:00:00 EDT 2016
· PLoS ONE
·
OSTI ID:1435827
+2 more
The Tp0684 (MglB-2) Lipoprotein of Treponema pallidum: A Glucose-Binding Protein with Divergent Topo
Journal Article
·
Mon Aug 01 00:00:00 EDT 2016
· PLoS One
·
OSTI ID:1435827
+1 more
The Tp0684 (MglB-2) Lipoprotein of Treponema pallidum: A Glucose-Binding Protein with Divergent Topo
Journal Article
·
Mon Aug 01 00:00:00 EDT 2016
· PLoS One
·
OSTI ID:1435827
+1 more