4W75

Crystal Structure of Full-Length Split GFP Mutant D21H/K26C Disulfide and Metal-Mediated Dimer, P 21 21 21 Space Group, Form 1

Summary for 4W75

• Entry DOI: 10.2210/pdb4w75/pdb
• Related: 4W69 4W6A 4W6B 4W6C 4W6D 4W6F 4W6G 4W6H 4W6I 4W6J 4W6K 4W6L 4W6M 4W6N 4W6O 4W6P 4W6R 4W6S 4W6T 4W6U 4W72 4W73 4W74 4W76 4W77 4W7A 4W7C 4W7D 4W7E 4W7F 4W7R 4W7X
• Descriptor: fluorescent protein D21H/K26C, COPPER (II) ION (2 entities in total)
• Functional Keywords: fluorescent protein
• Biological source: synthetic construct
• Total number of polymer chains: 2
• Total formula weight: 52234.34

Authors

Leibly, D.J.,Waldo, G.S.,Yeates, T.O. (deposition date: 2014-08-21, release date: 2015-03-04, Last modification date: 2024-10-30)

Primary citation

Leibly, D.J.,Arbing, M.A.,Pashkov, I.,DeVore, N.,Waldo, G.S.,Terwilliger, T.C.,Yeates, T.O.
A Suite of Engineered GFP Molecules for Oligomeric Scaffolding.
Structure, 23:1754-1768, 2015

PubMed Abstract: Applications ranging from synthetic biology to protein crystallization could be advanced by facile systems for connecting multiple proteins together in predefined spatial relationships. One approach to this goal is to engineer many distinct assembly forms of a single carrier protein or scaffold, to which other proteins of interest can then be readily attached. In this work we chose GFP as a scaffold and engineered many alternative oligomeric forms, driven by either specific disulfide bond formation or metal ion addition. We generated a wide range of spatial arrangements of GFP subunits from 11 different oligomeric variants, and determined their X-ray structures in a total of 33 distinct crystal forms. Some of the oligomeric GFP variants show geometric polymorphism depending on conditions, while others show considerable geometric rigidity. Potential future applications of this system are discussed.

PubMed: 26278175
DOI: 10.1016/j.str.2015.07.008

Experimental method

X-RAY DIFFRACTION (3.473 Å)