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dc.contributor.authorCAFFREY, MARTINen
dc.date.accessioned2015-05-19T15:02:35Z
dc.date.available2015-05-19T15:02:35Z
dc.date.issued2014en
dc.date.submitted2014en
dc.identifier.citationNji, E. Li, D. Doyle, D.A. Caffrey, M., Cloning, expression, purification, crystallization and preliminary X-ray diffraction of a lysine-specific permease from Pseudomonas aeruginosa, Acta Crystallographica Section F Structural Biology Communications, 70, 2014, 1362 - 1367en
dc.identifier.otherYen
dc.identifier.urihttp://hdl.handle.net/2262/73960
dc.descriptionPUBLISHEDen
dc.description.abstractThe prokaryotic lysine-specific permease (LysP) belongs to the amino acid– polyamine–organocation (APC) transporter superfamily. In the cell, members of this family are responsible for the uptake and recycling of nutrients, for the maintenance of a constant internal ion concentration and for cell volume regulation. The detailed mechanism of substrate selectivity and transport of l -lysine by LysP is not understood. A high-resolution crystal structure would enormously facilitate such an understanding. To this end, LysP from Pseudomonas aeruginosa was recombinantly expressed in Escherichia coli and purified to near homogeneity by immobilized metal ion-affinity chromatography (IMAC) and size-exclusion chromatography (SEC). Hexagonal- and rod-shaped crystals were obtained in the presence of l -lysine and the l -lysine analogue l -4- thialysine by vapour diffusion and diffracted to 7.5 A ̊ resolution. The diffraction data were indexed in space group P 2 1 , with unit-cell parameters a = 169.53, b = 169.53, c = 290.13 A ̊ , = 120en
dc.description.sponsorshipThis work was supported by grants from the Science Foundation Ireland (12/IA/1255) and the National Institutes of Health (GM75915, P50GM073210 and U54GM094599). Special thanks go to D. Drew, Stockholm University for the pWaldo GFPd and TEV protease expression vectors, to F. O’Gara, University College Cork for the P. aeruginosa PAO1 cells and to D. Aragao, V. Pye and A. Khan for help at the synchrotronen
dc.format.extent1362en
dc.format.extent1367en
dc.relation.ispartofseriesActa Crystallographica Section F Structural Biology Communicationsen
dc.relation.ispartofseries70en
dc.rightsYen
dc.subjectamino acid– polyamine–organocation (APC)en
dc.subject.lcshamino acid– polyamine–organocation (APC)en
dc.titleCloning, expression, purification, crystallization and preliminary X-ray diffraction of a lysine-specific permease from Pseudomonas aeruginosaen
dc.typeJournal Articleen
dc.contributor.sponsorScience Foundation Ireland (SFI)en
dc.type.supercollectionscholarly_publicationsen
dc.type.supercollectionrefereed_publicationsen
dc.identifier.peoplefinderurlhttp://people.tcd.ie/mcaffreen
dc.identifier.rssinternalid102689en
dc.identifier.doihttp://dx.doi.org/10.1107/S2053230X14017865en
dc.rights.ecaccessrightsopenAccess
dc.contributor.sponsorGrantNumber12/IA/125en
dc.identifier.rssurihttp://www.scopus.com/inward/record.url?eid=2-s2.0-84927517266&partnerID=40&md5=af06021b6904cfc4e65053e858816752en


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