1r73

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

spinqualitylabelsall models 1r73 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1r73 is a 1 chain structure with sequence from Thermotoga maritima. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function RL29_THEMA Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosomal protein L29

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