1R73

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

Summary for 1R73

• Entry DOI: 10.2210/pdb1r73/pdb
• NMR Information: BMRB: 5977
• Descriptor: 50S ribosomal protein L29 (1 entity in total)
• Functional Keywords: ribosome, structural genomics, psi, protein structure initiative, joint center for structural genomics, jcsg
• Biological source: Thermotoga maritima
• Total number of polymer chains: 1
• Total formula weight: 7989.50

Authors

Peti, W.,Etezady-Esfarjani, T.,Herrmann, T.,Klock, H.E.,Lesley, S.A.,Wuethrich, K.,Joint Center for Structural Genomics (JCSG) (deposition date: 2003-10-17, release date: 2004-08-10, Last modification date: 2024-05-22)

Primary citation

Peti, W.,Etezady-Esfarjani, T.,Herrmann, T.,Klock, H.E.,Lesley, S.A.,Wuethrich, K.
NMR for structural proteomics of Thermotoga maritima: Screening and structure determination
J.STRUCT.FUNCT.GENOM., 5:205-215, 2004

PubMed Abstract: 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.

PubMed: 15263836
DOI: 10.1023/B:JSFG.0000029055.84242.9f

Experimental method

SOLUTION NMR