3hap

Crystal structure of bacteriorhodopsin mutant L111A crystallized from bicelles

spinqualitylabelsall models 3hap, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3hap is a 1 chain structure with sequence from "bacillus_halobius_ruber"_klebahn_1919 "bacillus halobius ruber" klebahn 1919. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CPS, D10, D12, DD9, HP6, R16, RET Related: 3han, 3hao, 3haq, 3har, 3has Gene: bop, VNG_1467G ("Bacillus halobius ruber" Klebahn 1919) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BACR_HALSA] Light-driven proton pump. 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 A major driving force for water-soluble protein folding is the hydrophobic effect, but membrane proteins cannot make use of this stabilizing contribution in the apolar core of the bilayer. It has been proposed that membrane proteins compensate by packing more efficiently. We therefore investigated packing contributions experimentally by observing the energetic and structural consequences of cavity creating mutations in the core of a membrane protein. We observed little difference in the packing energetics of water and membrane soluble proteins. Our results imply that other mechanisms are employed to stabilize the structure of membrane proteins. Similar energetic contributions of packing in the core of membrane and water-soluble proteins.,Joh NH, Oberai A, Yang D, Whitelegge JP, Bowie JU J Am Chem Soc. 2009 Aug 12;131(31):10846-7. PMID:19603754 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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