Structural highlights
Function
[P37_MYCGE] P37 is part of a high-affinity transport system.
Publication Abstract from PubMed
Mycoplasma genitalium is one of the smallest organisms capable of self-replication and its sequence is considered a starting point for understanding the minimal genome required for life. MG289, a putative phosphonate substrate binding protein, is considered to be one of these essential genes. The crystal structure of MG289 has been solved at 1.95 A resolution. The structurally identified thiamine binding region reveals possible mechanisms for ligand promiscuity. MG289 was determined to be an extracytoplasmic thiamine binding lipoprotein. Computational analysis, size exclusion chromatography, and small angle X-ray scattering indicates that MG289 homodimerizes in a concentration-dependant manner. Comparisons to the thiamine pyrophosphate binding homolog Cypl reveal insights into the metabolic differences between mycoplasmal species including identifying possible kinases for cofactor phosphorylation and describing the mechanism of thiamine transport into the cell. These results provide a baseline to build our understanding of the minimal metabolic requirements of a living organism. Proteins 2011. (c) 2010 Wiley-Liss, Inc.
Insights into Mycoplasma genitalium metabolism revealed by the structure of MG289, an extracytoplasmic thiamine binding lipoprotein.,Sippel KH, Venkatakrishnan B, Boehlein SK, Sankaran B, Quirit JG, Govindasamy L, Agbandje-McKenna M, Goodison S, Rosser CJ, McKenna R Proteins. 2011 Feb;79(2):528-36. PMID:21117240[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sippel KH, Venkatakrishnan B, Boehlein SK, Sankaran B, Quirit JG, Govindasamy L, Agbandje-McKenna M, Goodison S, Rosser CJ, McKenna R. Insights into Mycoplasma genitalium metabolism revealed by the structure of MG289, an extracytoplasmic thiamine binding lipoprotein. Proteins. 2011 Feb;79(2):528-36. PMID:21117240 doi:10.1002/prot.22900
