3O39

Crystal Structure of SPY

Summary for 3O39

• Entry DOI: 10.2210/pdb3o39/pdb
• Descriptor: Periplasmic protein related to spheroblast formation, CADMIUM ION (3 entities in total)
• Functional Keywords: alpha-helical, structural genomics, montreal-kingston bacterial structural genomics initiative, bsgi, chaperone
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 27189.35

Authors

Ruane, K.M.,Shi, R.,Cygler, M.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2010-07-23, release date: 2011-02-16, Last modification date: 2024-11-06)

Primary citation

Quan, S.,Koldewey, P.,Tapley, T.,Kirsch, N.,Ruane, K.M.,Pfizenmaier, J.,Shi, R.,Hofmann, S.,Foit, L.,Ren, G.,Jakob, U.,Xu, Z.,Cygler, M.,Bardwell, J.C.
Genetic selection designed to stabilize proteins uncovers a chaperone called Spy.
Nat.Struct.Mol.Biol., 18:262-269, 2011

PubMed Abstract: To optimize the in vivo folding of proteins, we linked protein stability to antibiotic resistance, thereby forcing bacteria to effectively fold and stabilize proteins. When we challenged Escherichia coli to stabilize a very unstable periplasmic protein, it massively overproduced a periplasmic protein called Spy, which increases the steady-state levels of a set of unstable protein mutants up to 700-fold. In vitro studies demonstrate that the Spy protein is an effective ATP-independent chaperone that suppresses protein aggregation and aids protein refolding. Our strategy opens up new routes for chaperone discovery and the custom tailoring of the in vivo folding environment. Spy forms thin, apparently flexible cradle-shaped dimers. The structure of Spy is unlike that of any previously solved chaperone, making it the prototypical member of a new class of small chaperones that facilitate protein refolding in the absence of energy cofactors.

PubMed: 21317898
DOI: 10.1038/nsmb.2016

Experimental method

X-RAY DIFFRACTION (2.599 Å)