4aui

STRUCTURE AND FUNCTION OF THE PORB PORIN FROM DISSEMINATING N. GONORRHOEAE

spinqualitylabelsall models 4aui, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4aui is a 6 chain structure with sequence from Neisseria gonorrhoeae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Ligands: ATP, MG, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q51056_NEIGO Publication Abstract from PubMed The outer membrane of Gram-negative bacteria contains a large number of channel forming proteins, porins, for the uptake of small nutrient molecules. N. gonorrhoeae porins of the serotype A (PorBIA) are associated with disseminating diseases and mediate a rapid bacterial invasion into host cells in a phosphate-sensitive manner. To gain insights into this structure-function relationship we analyzed PorBIA by X-ray crystallography in the presence of phosphate and ATP. The structure of PorBIA in the complex solved at a resolution of 3.3 A displays a surplus of positive charges inside the channel. ATP ligand binding in the channel is coordinated by positively charged residues of the channel interior. These residues are ligating the aromatic, sugar and pyrophosphate moieties of the ligand. Two phosphate ions were observed in the structure, one of which clamped by two arginine residues (R92 and R124) localized at the extraplasmic channel exit. A short b-bulge in the b2-strand together with the long L3 loop narrow the barrel diameter significantly and further support substrate specificity through H-bond interactions. Interestingly, the structure also comprised a small peptide as remnant of a periplasmic protein which physically links porin molecules to the peptidoglycan network. To test the importance of R92 on bacterial invasion the residue was mutated. In vivo assays of bacteria carrying the R92S mutation confirmed the importance of this residue for host cell invasion. Furthermore, systematic sequence and structure comparisons of PorBIA from Neisseriaceae indicated the R92 residue to be unique in disseminating N. gonorrhoeae thereby possibly distinguishing invasion-promoting porins from other neisserial porins. Structure and function of the PorB porin from disseminating N. gonorrhoeae.,Zeth K, Kozjak-Pavlovic V, Faulstich M, Fraunholz M, Hurwitz R, Kepp O, Rudel T Biochem J. 2012 Oct 25. PMID:23095086 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porin 3D structures

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