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1UUN

Main porin from Mycobacterium smegmatis (MspA)

Summary for 1UUN
Entry DOI10.2210/pdb1uun/pdb
DescriptorMSPA (2 entities in total)
Functional Keywordsporin, mycobacteria
Biological sourceMYCOBACTERIUM SMEGMATIS
Total number of polymer chains2
Total formula weight38999.03
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 citationFaller, 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: 14976314
DOI: 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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