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1TE4

Solution structure of MTH187. Ontario Centre for Structural Proteomics target MTH0187_1_111; Northeast Structural Genomics Target TT740

Summary for 1TE4
Entry DOI10.2210/pdb1te4/pdb
Descriptorconserved protein MTH187 (1 entity in total)
Functional Keywordsmth187, methanobacterium thermoautotrophicum, structural proteomics, heat-like repeat, structural genomics, ocsp, nesg, protein structure initiative, psi, northeast structural genomics consortium, unknown function
Biological sourceMethanothermobacter thermautotrophicus
Total number of polymer chains1
Total formula weight14582.25
Authors
Gignac, I.,Julien, O.,Yee, A.,Arrowsmith, C.H.,Gagne, S.M.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2004-05-24, release date: 2004-07-13, Last modification date: 2024-05-22)
Primary citationJulien, O.,Gignac, I.,Hutton, A.,Yee, A.,Arrowsmith, C.H.,Gagne, S.M.
MTH187 from Methanobacterium thermoautotrophicum has three HEAT-like Repeats.
J.Biomol.Nmr, 35:149-154, 2006
Cited by
PubMed Abstract: With the completion of genome sequencing projects, there are a large number of proteins for which we have little or no functional information. Since protein function is closely related to three-dimensional conformation, structural proteomics is one avenue where the role of proteins with unknown function can be investigated. In the present structural project, the structure of MTH187 has been determined by solution-state NMR spectroscopy. This protein of 12.4 kDa is one of the 424 non-membrane proteins that were cloned and purified for the structural proteomic project of Methanobacterium thermoautotrophicum [Christendat, D., Yee, A., Dharamsi, A., Kluger, Y., Gerstein, M., Arrowsmith, C.H. and Edwards, A.M. (2000) Prog. Biophys. Mol. Biol., 73, 339-345]. Methanobacterium thermoautotrophicum is a thermophilic archaeon that grows optimally at 65 degrees C. A particular characteristic of this microorganism is its ability to generate methane from carbon dioxide and hydrogen [Smith, D.R., Doucette-Stamm, L.A., Deloughery, C., Lee, H., Dubois, J., Aldredge, T., Bashirzadeh, R., Blakely, D., Cook, R., Gilbert, K., Harrison, D., Hoang, L., Keagle, P., Lumm, W., Pothier, B., Qiu, D., Spadafora, R., Vicaire, R., Wang, Y., Wierzbowski, J., Gibson, R., Jiwani, N., Caruso, A., Bush, D., Reeve, J. N. et al. (1997) J. Bacteriol., 179, 7135-7155].
PubMed: 16819590
DOI: 10.1007/s10858-006-0029-3
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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