1r73

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Solution Structure of TM1492, the L29 ribosomal protein from Thermotoga maritima

Overview

This paper describes the NMR screening of 141 small (<15 kDa) recombinant, Thermotoga maritima proteins for globular folding. The experimental data, shows that approximately 25% of the screened proteins are folded under our, screening conditions, which makes this procedure an important step for, selecting those proteins that are suitable for structure determination. A, comparison of screening based either on 1D 1H NMR with unlabeled proteins, or on 2D [1H,15N]-COSY with uniformly 15N-labeled proteins is presented, and a comprehensive analysis of the 1D 1H NMR screening data is described., As an illustration of the utility of these methods to structural, proteomics, the NMR structure determination of TM1492 (ribosomal protein, L29) is presented. This 66-residue protein consists of a N-terminal, 3(10)-helix and two long alpha-helices connected by a tight turn centered, about glycine 35, where conserved leucine and isoleucine residues in the, two alpha-helices form a small hydrophobic core.

About this Structure

1R73 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

NMR for structural proteomics of Thermotoga maritima: screening and structure determination., Peti W, Etezady-Esfarjani T, Herrmann T, Klock HE, Lesley SA, Wuthrich K, J Struct Funct Genomics. 2004;5(3):205-15. PMID:15263836

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