5XFU
Domain swapped dimer crystal structure of loop1 deletion mutant in Single-chain Monellin
Summary for 5XFU
| Entry DOI | 10.2210/pdb5xfu/pdb |
| Descriptor | Monellin chain B,Monellin chain A (1 entity in total) |
| Functional Keywords | domain swapped dimer, single-chain monellin, hinge loop composition, loop deletion, plant protein |
| Biological source | Dioscoreophyllum cumminsii (Serendipity berry) More |
| Total number of polymer chains | 5 |
| Total formula weight | 54852.97 |
| Authors | Surana, P.,Nandwani, N.,Udgaonkar, J.,Gosavi, S.,Das, R. (deposition date: 2017-04-11, release date: 2017-07-26, Last modification date: 2023-11-22) |
| Primary citation | Nandwani, N.,Surana, P.,Udgaonkar, J.B.,Das, R.,Gosavi, S. Amino-acid composition after loop deletion drives domain swapping Protein Sci., 26:1994-2002, 2017 Cited by PubMed Abstract: 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 β-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. PubMed: 28710790DOI: 10.1002/pro.3237 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.611 Å) |
Structure validation
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