5APP

Actinobacillus actinomycetemcomitans OMP100 residues 133-198 fused to GCN4 adaptors

Summary for 5APP

• Entry DOI: 10.2210/pdb5app/pdb
• Related: 5APQ 5APS 5APT 5APU 5APV 5APW 5APX 5APY 5APZ
• Descriptor: General control protein GCN4,GENERAL CONTROL PROTEIN GCN4, OUTER MEMBRANE PROTEIN 100,General control protein GCN4, CHLORIDE ION (3 entities in total)
• Functional Keywords: membrane protein, fusion protein, alpha/beta coiled coil, beta layer, trimer, chimera
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Total number of polymer chains: 3
• Total formula weight: 46502.45

Authors

Hartmann, M.D.,Ridderbusch, O.,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

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: 26771248
DOI: 10.7554/eLife.11861

Experimental method

X-RAY DIFFRACTION (2.3 Å)