1JCU
Solution Structure of MTH1692 Protein from Methanobacterium thermoautotrophicum
Summary for 1JCU
| Entry DOI | 10.2210/pdb1jcu/pdb |
| NMR Information | BMRB: 5051 |
| Descriptor | conserved protein MTH1692 (1 entity in total) |
| Functional Keywords | mixed alpha-beta structure, structural genomics |
| Biological source | Methanothermobacter thermautotrophicus |
| Total number of polymer chains | 1 |
| Total formula weight | 22642.18 |
| Authors | Kozlov, G.,Ekiel, I.,Gehring, K. (deposition date: 2001-06-11, release date: 2002-07-24, Last modification date: 2024-05-22) |
| Primary citation | Yee, A.,Chang, X.,Pineda-Lucena, A.,Wu, B.,Semesi, A.,Le, B.,Ramelot, T.,Lee, G.M.,Bhattacharyya, S.,Gutierrez, P.,Denisov, A.,Lee, C.H.,Cort, J.R.,Kozlov, G.,Liao, J.,Finak, G.,Chen, L.,Wishart, D.,Lee, W.,McIntosh, L.P.,Gehring, K.,Kennedy, M.A.,Edwards, A.M.,Arrowsmith, C.H. An NMR approach to structural proteomics. Proc.Natl.Acad.Sci.USA, 99:1825-1830, 2002 Cited by PubMed Abstract: The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMR. Although there was variability among proteomes, overall 20% of these proteins were found to be readily amenable to NMR structure determination. NMR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins. PubMed: 11854485DOI: 10.1073/pnas.042684599 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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