1mkh
From Proteopedia
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C-terminal domain of methionyl-tRNA synthetase from Pyrococcus abyssi
Overview
The minimal polypeptide supporting full methionyl-tRNA synthetase (MetRS), activity is composed of four domains: a catalytic Rossmann fold, a, connective peptide, a KMSKS domain, and a C-terminal alpha helix bundle, domain. The minimal MetRS behaves as a monomer. In several species, MetRS, is a homodimer because of a C-terminal domain appended to the core, polypeptide. Upon truncation of this C-terminal domain, subunits, dissociate irreversibly. Here, the C-terminal domain of dimeric MetRS from, Pyrococcus abyssi was isolated and studied. It displays nonspecific, tRNA-binding properties and has a crystalline structure closely resembling, that of Trbp111, a dimeric tRNA-binding protein found in many bacteria and, archaea. The obtained 3D model was used to direct mutations against, dimerization of Escherichia coli MetRS. Comparison of the resulting, mutants to native and C-truncated MetRS shows that the presence of the, appended C-domain improves tRNA(Met) binding affinity. However, dimer, formation is required to evidence the gain in affinity.
About this Structure
1MKH is a Single protein structure of sequence from Pyrococcus abyssi. Active as Methionine--tRNA ligase, with EC number 6.1.1.10 Full crystallographic information is available from OCA.
Reference
Structure and function of the C-terminal domain of methionyl-tRNA synthetase., Crepin T, Schmitt E, Blanquet S, Mechulam Y, Biochemistry. 2002 Oct 29;41(43):13003-11. PMID:12390027
Page seeded by OCA on Tue Nov 20 21:28:42 2007
