1GAM

GAMMA B CRYSTALLIN TRUNCATED C-TERMINAL DOMAIN

Summary for 1GAM

• Entry DOI: 10.2210/pdb1gam/pdb
• Descriptor: GAMMA B CRYSTALLIN (2 entities in total)
• Functional Keywords: gamma crystallin b, eye lens protein, multigene family, eye-lens protein
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 2
• Total formula weight: 20705.55

Authors

Norledge, B.V.,Mayr, E.-M.,Glockshuber, R.,Bateman, O.A.,Slingsby, C.,Jaenicke, R.,Driessen, H.P.C. (deposition date: 1996-02-02, release date: 1996-07-11, Last modification date: 2024-02-07)

Primary citation

Norledge, B.V.,Mayr, E.M.,Glockshuber, R.,Bateman, O.A.,Slingsby, C.,Jaenicke, R.,Driessen, H.P.
The X-ray structures of two mutant crystallin domains shed light on the evolution of multi-domain proteins.
Nat.Struct.Biol., 3:267-274, 1996

PubMed Abstract: We use protein engineering and crystallography to simulate aspects of the early evolution of beta gamma-crystallins by observing how a single domain oligomerizes in response to changes in a sequence extension. The crystal structure of the C-terminal domain of gamma beta-crystallin with its four-residue C-terminal extension shows that the domain does not form a symmetric homodimer analogous to the two-domain pairing in beta gamma-crystallins. Instead the C-terminal extension now forms heterologous interactions with other domains leading to the solvent exposure of the natural hydrophobic interface with a consequent loss in protein solubility. However, this domain truncated by just the C-terminal tyrosine forms a symmetric homodimer of domains in the crystal lattice.

PubMed: 8605629
DOI: 10.1038/nsb0396-267

Experimental method

X-RAY DIFFRACTION (2.6 Å)