1uun

MAIN PORIN FROM MYCOBACTERIA SMEGMATIS (MSPA)MAIN PORIN FROM MYCOBACTERIA SMEGMATIS (MSPA)

Structural highlights 1uun is a 2 chain structure with sequence from Mycobacterium smegmatis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porin

spinqualitylabelsall models 1uun, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image