5EWX
Fusion protein of T4 lysozyme and B4 domain of protein A from staphylococcal aureus with chemical cross-linker EY-CBS
Summary for 5EWX
| Entry DOI | 10.2210/pdb5ewx/pdb |
| Descriptor | Endolysin,Immunoglobulin G-binding protein A,Endolysin, 2,2'-ethyne-1,2-diylbis{5-[(chloroacetyl)amino]benzenesulfonic acid} (3 entities in total) |
| Functional Keywords | fusion, ey-cbs, alpha helix, cross-linker, protein binding |
| Biological source | Enterobacteria phage T4 More |
| Cellular location | Host cytoplasm : P00720 |
| Total number of polymer chains | 2 |
| Total formula weight | 51467.63 |
| Authors | Jeong, W.H.,Lee, H.,Song, D.H.,Lee, J.O. (deposition date: 2015-11-22, release date: 2016-03-30, Last modification date: 2023-11-08) |
| Primary citation | Jeong, W.H.,Lee, H.,Song, D.H.,Eom, J.H.,Kim, S.C.,Lee, H.S.,Lee, H.,Lee, J.O. Connecting two proteins using a fusion alpha helix stabilized by a chemical cross linker. Nat Commun, 7:11031-11031, 2016 Cited by PubMed Abstract: Building a sophisticated protein nano-assembly requires a method for linking protein components in a predictable and stable structure. Most of the cross linkers available have flexible spacers. Because of this, the linked hybrids have significant structural flexibility and the relative structure between their two components is largely unpredictable. Here we describe a method of connecting two proteins via a 'fusion α helix' formed by joining two pre-existing helices into a single extended helix. Because simple ligation of two helices does not guarantee the formation of a continuous helix, we used EY-CBS, a synthetic cross linker that has been shown to react selectively with cysteines in α-helices, to stabilize the connecting helix. Formation and stabilization of the fusion helix was confirmed by determining the crystal structures of the fusion proteins with and without bound EY-CBS. Our method should be widely applicable for linking protein building blocks to generate predictable structures. PubMed: 26980593DOI: 10.1038/ncomms11031 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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