3b1y

Crystal structure of an S. thermophilus NFeoB T35A mutant bound to GDP

spinqualitylabelsall models 3b1y, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3b1y is a 1 chain structure with sequence from Streptococcus thermophilus LMG 18311. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Ligands: GNH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5M586_STRT2 Publication Abstract from PubMed The acquisition of ferrous iron in prokaryotes is achieved by the G-protein-coupled membrane protein FeoB. This protein possesses a large C-terminal membrane-spanning domain preceded by two soluble cytoplasmic domains that are together termed 'NFeoB'. The first of these soluble domains is a GTPase domain (G-domain), which is then followed by an entirely alpha-helical domain. GTP hydrolysis by the G-domain is essential for iron uptake by FeoB, and various NFeoB mutant proteins from Streptococcus thermophilus have been constructed. These mutations investigate the role of conserved amino acids from the protein's critical Switch regions. Five crystal structures of these mutant proteins have been determined. The structures of E66A and E67A mutant proteins were solved in complex with nonhydrolyzable GTP analogues, the structures of T35A and E67A mutant proteins were solved in complex with GDP and finally the structure of the T35S mutant was crystallized without bound nucleotide. As an ensemble, the structures illustrate how small nucleotide-dependent rearrangements at the active site are converted into large rigid-body reorientations of the helical domain in response to GTP binding and hydrolysis. This provides the first evidence of nucleotide-dependent helical domain movement in NFeoB proteins, suggesting a mechanism by which the G-protein domain could structurally communicate with the membrane domain and mediate iron uptake. A suite of Switch I and Switch II mutant structures from the G-protein domain of FeoB.,Ash MR, Maher MJ, Guss JM, Jormakka M Acta Crystallogr D Biol Crystallogr. 2011 Nov;67(Pt 11):973-80. Epub 2011 Oct 19. PMID:22101824 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA