5xfu | pdb_00005xfu

Domain swapped dimer crystal structure of loop1 deletion mutant in Single-chain Monellin

spinqualitylabelsall models 5xfu, resolution 2.61Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xfu is a 5 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MONB_DIOCU] Taste-modifying protein; intensely sweet-tasting protein. Publication Abstract from PubMed Rational engineering of a protein to enable domain swapping requires an understanding of the sequence, structural and energetic factors that favor the domain-swapped oligomer over the monomer. While it is known that the deletion of loops between beta-strands can promote domain swapping, the spliced sequence at the position of the loop deletion is thought to have a minimal role to play in such domain swapping. Here, two loop-deletion mutants of the non-domain-swapping protein monellin, frame-shifted by a single residue, were designed. Although the spliced sequence in the two mutants differed by only one residue at the site of the deletion, only one of them (YEIKG) promoted domain swapping. The mutant containing the spliced sequence YENKG was entirely monomeric. This new understanding that the domain swapping propensity after loop deletion may depend critically on the chemical composition of the shortened loop will facilitate the rational design of domain swapping. Amino-acid composition after loop deletion drives domain swapping.,Nandwani N, Surana P, Udgaonkar JB, Das R, Gosavi S Protein Sci. 2017 Oct;26(10):1994-2002. doi: 10.1002/pro.3237. Epub 2017 Aug 30. PMID:28710790 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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