5APT
Sequence IENKADKAD inserted between GCN4 adaptors - Structure A9
Summary for 5APT
| Entry DOI | 10.2210/pdb5apt/pdb |
| Related | 5APP 5APQ 5APS 5APU 5APV 5APW 5APX 5APY 5APZ |
| Descriptor | GENERAL CONTROL PROTEIN GCN4 (2 entities in total) |
| Functional Keywords | structural protein, alpha/beta coiled coil, beta layer, trimer |
| Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) |
| Cellular location | Nucleus: P03069 |
| Total number of polymer chains | 3 |
| Total formula weight | 34182.23 |
| Authors | Hartmann, M.D.,Mendler, C.T.,Lupas, A.N.,Hernandez Alvarez, B. (deposition date: 2015-09-17, release date: 2016-01-27, Last modification date: 2024-01-10) |
| Primary citation | Hartmann, M.D.,Mendler, C.T.,Bassler, J.,Karamichali, I.,Ridderbusch, O.,Lupas, A.N.,Hernandez Alvarez, B. alpha / beta coiled coils. Elife, 5:-, 2016 Cited by PubMed Abstract: Coiled coils are the best-understood protein fold, as their backbone structure can uniquely be described by parametric equations. This level of understanding has allowed their manipulation in unprecedented detail. They do not seem a likely source of surprises, yet we describe here the unexpected formation of a new type of fiber by the simple insertion of two or six residues into the underlying heptad repeat of a parallel, trimeric coiled coil. These insertions strain the supercoil to the breaking point, causing the local formation of short β-strands, which move the path of the chain by 120° around the trimer axis. The result is an α/β coiled coil, which retains only one backbone hydrogen bond per repeat unit from the parent coiled coil. Our results show that a substantially novel backbone structure is possible within the allowed regions of the Ramachandran space with only minor mutations to a known fold. PubMed: 26771248DOI: 10.7554/eLife.11861 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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