1UUN
Main porin from Mycobacterium smegmatis (MspA)
Summary for 1UUN
Entry DOI | 10.2210/pdb1uun/pdb |
Descriptor | MSPA (2 entities in total) |
Functional Keywords | porin, mycobacteria |
Biological source | MYCOBACTERIUM SMEGMATIS |
Total number of polymer chains | 2 |
Total formula weight | 38999.03 |
Authors | Faller, M.,Niederweis, M.,Schulz, G.E. (deposition date: 2004-01-08, release date: 2004-02-26, Last modification date: 2024-05-08) |
Primary citation | Faller, M.,Niederweis, M.,Schulz, G.E. The Structure of a Mycobacterial Outer-Membrane Channel Science, 303:1189-, 2004 Cited by PubMed Abstract: 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. PubMed: 14976314DOI: 10.1126/SCIENCE.1094114 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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