4nlj

Crystal structure of sheep beta-lactoglobulin (space group P1)

spinqualitylabelsall models 4nlj, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4nlj is a 2 chain structure with sequence from Ovis aries. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 4nli Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LACB_SHEEP] Lactoglobulin is the primary component of whey, it binds retinol and is probably involved in the transport of that molecule. Publication Abstract from PubMed Ovine beta-lactoglobulin has been isolated from whey fraction of sheep milk and crystallized. The high-resolution structures of two crystal forms (triclinic and trigonal) obtained at pH 7.0 have been determined revealing that ovine protein, similarly to its bovine analog, is dimeric. Access to the binding site located in the eight-stranded antiparallel beta-barrel in both structures is blocked by the EF loop that has been found in closed conformation. Similarly to bovine lactoglobulin (BLG), conformation of the EF loop is stabilized by hydrogen bond between Glu89 and Ser116 indicating that Tanford transition might occur with the same mechanism. The substitution at six positions in relation to the most abundant isoform B of BLG also affects the distribution of electrostatic potentials and the total charge. (c) 2014 Wiley Periodicals, Inc. Biopolymers 101: 886-894, 2014. Structure of two crystal forms of sheep beta-lactoglobulin with EF-loop in closed conformation.,Loch JI, Molenda M, Kopec M, Swiatek S, Lewinski K Biopolymers. 2014 Aug;101(8):886-94. doi: 10.1002/bip.22471. PMID:25098178 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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