2WW7

foldon containing beta-turn mimic

Summary for 2WW7

• Entry DOI: 10.2210/pdb2ww7/pdb
• Related: 2WW6
• Descriptor: FIBRITIN (2 entities in total)
• Functional Keywords: d-amino acids, chaperone, viral protein
• Biological source: ENTEROBACTERIA PHAGE T4
• Total number of polymer chains: 6
• Total formula weight: 18819.72

Authors

Eckhardt, B.,Grosse, W.,Essen, L.-O.,Geyer, A. (deposition date: 2009-10-22, release date: 2010-09-29, Last modification date: 2023-12-20)

Primary citation

Eckhardt, B.,Grosse, W.,Essen, L.,Geyer, A.
Structural Characterization of a Beta-Turn Mimic within a Protein-Protein Interface.
Proc.Natl.Acad.Sci.USA, 107:18336-, 2010

PubMed Abstract: β-Turns are secondary structure elements not only exposed on protein surfaces, but also frequently found to be buried in protein-protein interfaces. Protein engineering so far considered mainly the backbone-constraining properties of synthetic β-turn mimics as parts of surface-exposed loops. A β-turn mimic, Hot═Tap, that is available in gram amounts, provides two hydroxyl groups that enhance its turn-inducing properties besides being able to form side-chain-like interactions. NMR studies on cyclic hexapeptides harboring the Hot═Tap dipeptide proved its strong β-turn-inducing capability. Crystallographic analyses of the trimeric fibritin-foldon/Hot═Tap hybrid reveal at atomic resolution how Hot═Tap replaces a βI'-turn by a βII'-type structure. Furthermore, Hot═Tap adapts to the complex protein environment by participating in several direct and water-bridged interactions across the foldon trimer interface. As building blocks, β-turn mimics capable of both backbone and side-chain mimicry may simplify the design of synthetic proteins.

PubMed: 20937907
DOI: 10.1073/PNAS.1004187107

Experimental method

X-RAY DIFFRACTION (1.06 Å)