1GME

Crystal structure and assembly of an eukaryotic small heat shock protein

Summary for 1GME

• Entry DOI: 10.2210/pdb1gme/pdb
• Descriptor: HEAT SHOCK PROTEIN 16.9B (2 entities in total)
• Functional Keywords: small heat shock protein, chaperone, alpha-crystallin
• Biological source: TRITICUM AESTIVUM (WHEAT)
• Cellular location: Cytoplasm : Q41560
• Total number of polymer chains: 4
• Total formula weight: 67524.67

Authors

Van Montfort, R.L.M.,Basha, E.,Friedrich, K.L.,Slingsby, C.,Vierling, E. (deposition date: 2001-09-13, release date: 2001-11-29, Last modification date: 2024-05-08)

Primary citation

Van Montfort, R.L.M.,Basha, E.,Friedrich, K.L.,Slingsby, C.,Vierling, E.
Crystal Structure and Assembly of an Eukaryotic Small Heat Shock Protein
Nat.Struct.Biol., 8:1025-, 2001

PubMed Abstract: The 2.7 A structure of wheat HSP16.9, a member of the small heat shock proteins (sHSPs), indicates how its alpha-crystallin domain and flanking extensions assemble into a dodecameric double disk. The folding of the monomer and assembly of the oligomer are mutually interdependent, involving strand exchange, helix swapping, loose knots and hinged extensions. In support of the chaperone mechanism, the substrate-bound dimers, in temperature-dependent equilibrium with higher assembly forms, have unfolded N-terminal arms and exposed conserved hydrophobic binding sites on the alpha-crystallin domain. The structure also provides a model by which members of the sHSP protein family bind unfolded substrates, which are involved in a variety of neurodegenerative diseases and cataract formation.

PubMed: 11702068
DOI: 10.1038/NSB722

Experimental method

X-RAY DIFFRACTION (2.7 Å)