Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Mycobacteria have low-permeability outer membranes that render them resistant to most antibiotics. Hydrophilic nutrients can enter by way of transmembrane-channel proteins called porins. An x-ray analysis of the main porin from Mycobacterium smegmatis, MspA, revealed a homooctameric goblet-like conformation with a single central channel. This is the first structure of a mycobacterial outer-membrane protein. No structure-related protein was found in the Protein Data Bank. MspA contains two consecutive beta barrels with nonpolar outer surfaces that form a ribbon around the porin, which is too narrow to fit the thickness of the mycobacterial outer membrane in contemporary models.
The structure of a mycobacterial outer-membrane channel.,Faller M, Niederweis M, Schulz GE Science. 2004 Feb 20;303(5661):1189-92. PMID:14976314[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Faller M, Niederweis M, Schulz GE. The structure of a mycobacterial outer-membrane channel. Science. 2004 Feb 20;303(5661):1189-92. PMID:14976314 doi:10.1126/science.1094114
