1pu1: Difference between revisions

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New page: left|200px<br /><applet load="1pu1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pu1" /> '''Solution structure of the Hypothetical prote...
 
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'''Solution structure of the Hypothetical protein mth677 from Methanothermobacter Thermautotrophicus'''<br />
'''Solution structure of the Hypothetical protein mth677 from Methanothermobacter Thermautotrophicus'''<br />


==Overview==
==Overview==
The structure of Mth677, a hypothetical protein from Methanobacterium, thermoautotrophicum (Mth), has been determined by using heteronuclear, nuclear magnetic resonance (NMR) methods on a double-labeled (15)N-(13)C, sample. Mth677 adopts a novel alpha+beta fold, consisting of two, alpha-helices (one N terminal and one C terminal) packed on the same side, of a central beta-hairpin. This structure is likely shared by its three, orthologs, detected in three other Archaebacteria. There are no clear, features in the sequences of these proteins or in the genome organization, of Mth to make a reliable functional assignment to this protein. However, the structural similarity to Escherichia coli MinE, the protein which, controls that division occurs at the midcell site, lends support to the, proposal that Mth677 might be, in Mth, the counterpart of the topological, specificity domain of MinE in E. coli.
The structure of Mth677, a hypothetical protein from Methanobacterium thermoautotrophicum (Mth), has been determined by using heteronuclear nuclear magnetic resonance (NMR) methods on a double-labeled (15)N-(13)C sample. Mth677 adopts a novel alpha+beta fold, consisting of two alpha-helices (one N terminal and one C terminal) packed on the same side of a central beta-hairpin. This structure is likely shared by its three orthologs, detected in three other Archaebacteria. There are no clear features in the sequences of these proteins or in the genome organization of Mth to make a reliable functional assignment to this protein. However, the structural similarity to Escherichia coli MinE, the protein which controls that division occurs at the midcell site, lends support to the proposal that Mth677 might be, in Mth, the counterpart of the topological specificity domain of MinE in E. coli.


==About this Structure==
==About this Structure==
1PU1 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PU1 OCA].  
1PU1 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=1PU1 OCA].  


==Reference==
==Reference==
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[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Arrowsmith, C.H.]]
[[Category: Arrowsmith, C H.]]
[[Category: Blanco, F.J.]]
[[Category: Blanco, F J.]]
[[Category: Campos-Olivas, R.]]
[[Category: Campos-Olivas, R.]]
[[Category: Devos, D.]]
[[Category: Devos, D.]]
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[[Category: structural genomics]]
[[Category: structural genomics]]


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Revision as of 15:32, 21 February 2008

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1pu1

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Solution structure of the Hypothetical protein mth677 from Methanothermobacter Thermautotrophicus

OverviewOverview

The structure of Mth677, a hypothetical protein from Methanobacterium thermoautotrophicum (Mth), has been determined by using heteronuclear nuclear magnetic resonance (NMR) methods on a double-labeled (15)N-(13)C sample. Mth677 adopts a novel alpha+beta fold, consisting of two alpha-helices (one N terminal and one C terminal) packed on the same side of a central beta-hairpin. This structure is likely shared by its three orthologs, detected in three other Archaebacteria. There are no clear features in the sequences of these proteins or in the genome organization of Mth to make a reliable functional assignment to this protein. However, the structural similarity to Escherichia coli MinE, the protein which controls that division occurs at the midcell site, lends support to the proposal that Mth677 might be, in Mth, the counterpart of the topological specificity domain of MinE in E. coli.

About this StructureAbout this Structure

1PU1 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.

ReferenceReference

Solution structure of the hypothetical protein Mth677 from Methanobacterium thermoautotrophicum: a novel alpha+beta fold., Blanco FJ, Yee A, Campos-Olivas R, Ortiz AR, Devos D, Valencia A, Arrowsmith CH, Rico M, Protein Sci. 2004 Jun;13(6):1458-65. PMID:15152082

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