1te4
From Proteopedia
(New page: 200px<br /><applet load="1te4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1te4" /> '''Solution structure of MTH187. Ontario Centre...) |
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| - | [[Image:1te4.jpg|left|200px]]<br /><applet load="1te4" size=" | + | [[Image:1te4.jpg|left|200px]]<br /><applet load="1te4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1te4" /> | caption="1te4" /> | ||
'''Solution structure of MTH187. Ontario Centre for Structural Proteomics target MTH0187_1_111; Northeast Structural Genomics Target TT740'''<br /> | '''Solution structure of MTH187. Ontario Centre for Structural Proteomics target MTH0187_1_111; Northeast Structural Genomics Target TT740'''<br /> | ||
==Overview== | ==Overview== | ||
| - | With the completion of genome sequencing projects, there are a large | + | 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]. |
==About this Structure== | ==About this Structure== | ||
| - | 1TE4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http:// | + | 1TE4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TE4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Methanothermobacter thermautotrophicus]] | [[Category: Methanothermobacter thermautotrophicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Arrowsmith, C | + | [[Category: Arrowsmith, C H.]] |
| - | [[Category: Gagne, S | + | [[Category: Gagne, S M.]] |
[[Category: Gignac, I.]] | [[Category: Gignac, I.]] | ||
[[Category: Julien, O.]] | [[Category: Julien, O.]] | ||
| - | [[Category: NESG, Northeast | + | [[Category: NESG, Northeast Structural Genomics Consortium.]] |
[[Category: Yee, A.]] | [[Category: Yee, A.]] | ||
[[Category: heat-like repeat]] | [[Category: heat-like repeat]] | ||
| Line 31: | Line 31: | ||
[[Category: structural proteomics]] | [[Category: structural proteomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:40 2008'' |
Revision as of 13:12, 21 February 2008
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Solution structure of MTH187. Ontario Centre for Structural Proteomics target MTH0187_1_111; Northeast Structural Genomics Target TT740
Overview
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].
About this Structure
1TE4 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.
Reference
MTH187 from Methanobacterium thermoautotrophicum has three HEAT-like repeats., Julien O, Gignac I, Hutton A, Yee A, Arrowsmith CH, Gagne SM, J Biomol NMR. 2006 Jun;35(2):149-54. Epub 2006 May 31. PMID:16819590
Page seeded by OCA on Thu Feb 21 15:12:40 2008
Categories: Methanothermobacter thermautotrophicus | Single protein | Arrowsmith, C H. | Gagne, S M. | Gignac, I. | Julien, O. | NESG, Northeast Structural Genomics Consortium. | Yee, A. | Heat-like repeat | Methanobacterium thermoautotrophicum | Mth187 | Nesg | Nmr | Northeast structural genomics consortium | Ocsp | Protein structure initiative | Psi | Structural genomics | Structural proteomics
