1EIJ
NMR ENSEMBLE OF METHANOBACTERIUM THERMOAUTOTROPHICUM PROTEIN 1615
Summary for 1EIJ
| Entry DOI | 10.2210/pdb1eij/pdb |
| Descriptor | HYPOTHETICAL PROTEIN MTH1615 (1 entity in total) |
| Functional Keywords | beta-helix, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, dna binding protein |
| Biological source | Methanothermobacter thermautotrophicus |
| Total number of polymer chains | 1 |
| Total formula weight | 9576.51 |
| Authors | Christendat, D.,Booth, V.,Gernstein, M.,Arrowsmith, C.H.,Edwards, A.M.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2000-02-25, release date: 2000-11-03, Last modification date: 2024-05-22) |
| Primary citation | Christendat, D.,Yee, A.,Dharamsi, A.,Kluger, Y.,Savchenko, A.,Cort, J.R.,Booth, V.,Mackereth, C.D.,Saridakis, V.,Ekiel, I.,Kozlov, G.,Maxwell, K.L.,Wu, N.,McIntosh, L.P.,Gehring, K.,Kennedy, M.A.,Davidson, A.R.,Pai, E.F.,Gerstein, M.,Edwards, A.M.,Arrowsmith, C.H. Structural proteomics of an archaeon. Nat.Struct.Biol., 7:903-909, 2000 Cited by PubMed Abstract: A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, approximately 20% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility, implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics. PubMed: 11017201DOI: 10.1038/82823 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
