3odj

Crystal structure of H. influenzae rhomboid GlpG with disordered loop 4, helix 5 and loop 5

spinqualitylabelsall models 3odj, resolution 2.84Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3odj is a 1 chain structure with sequence from "bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3b44, 3b45, 2o7l, 2nrf, 2irv, 2ic8 Gene: glpG, HI_0618 ("Bacterium influenzae" Lehmann and Neumann 1896) Activity: Rhomboid protease, with EC number 3.4.21.105 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [GLPG_HAEIN] Rhomboid-type serine protease that catalyzes intramembrane proteolysis (By similarity). Publication Abstract from PubMed Rhomboids are a remarkable class of serine proteases that are embedded in lipid membranes. These membrane-bound enzymes play key roles in cellular signaling events, and disruptions in these events can result in numerous disease pathologies, including hereditary blindness, type 2 diabetes, Parkinson's disease, and epithelial cancers. Recent crystal structures of rhomboids from Escherichia coli have focused on how membrane-bound substrates gain access to a buried active site. In E. coli, it has been shown that movements of loop 5, with smaller movements in helix 5 and loop 4, act as substrate gate, facilitating inhibitor access to rhomboid catalytic residues. Herein we present a new structure of the Haemophilus influenzae rhomboid hiGlpG, which reveals disorder in loop 5, helix 5, and loop 4, indicating that, together, they represent mobile elements of the substrate gate. Substrate cleavage assays by hiGlpG with amino acid substitutions in these mobile regions demonstrate that the flexibilities of both loop 5 and helix 5 are important for access of the substrates to the catalytic residues. Mutagenesis indicates that less mobility by loop 4 is required for substrate cleavage. A reexamination of the reaction mechanism of rhomboid substrates, whereby cleavage of the scissile bond occurs on the si-face of the peptide bond, is discussed. Insights into Substrate Gating in H. influenzae Rhomboid.,Brooks CL, Lazareno-Saez C, Lamoureux JS, Mak MW, Lemieux MJ J Mol Biol. 2011 Feb 3. PMID:21295583 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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