1eij: Difference between revisions

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New page: left|200px<br /><applet load="1eij" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eij" /> '''NMR ENSEMBLE OF METHANOBACTERIUM THERMOAUTOT...
 
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[[Image:1eij.gif|left|200px]]<br /><applet load="1eij" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1eij.gif|left|200px]]<br /><applet load="1eij" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1eij" />
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'''NMR ENSEMBLE OF METHANOBACTERIUM THERMOAUTOTROPHICUM PROTEIN 1615'''<br />
'''NMR ENSEMBLE OF METHANOBACTERIUM THERMOAUTOTROPHICUM PROTEIN 1615'''<br />


==Overview==
==Overview==
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.
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.


==About this Structure==
==About this Structure==
1EIJ 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=1EIJ OCA].  
1EIJ 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=1EIJ 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: Booth, V.]]
[[Category: Booth, V.]]
[[Category: Christendat, D.]]
[[Category: Christendat, D.]]
[[Category: Edwards, A.M.]]
[[Category: Edwards, A M.]]
[[Category: Gernstein, M.]]
[[Category: Gernstein, M.]]
[[Category: NESG, Northeast.Structural.Genomics.Consortium.]]
[[Category: NESG, Northeast Structural Genomics Consortium.]]
[[Category: beta-helix]]
[[Category: beta-helix]]
[[Category: nesg]]
[[Category: nesg]]
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[[Category: structural genomics]]
[[Category: structural genomics]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:06 2008''

Revision as of 13:28, 21 February 2008

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1eij

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NMR ENSEMBLE OF METHANOBACTERIUM THERMOAUTOTROPHICUM PROTEIN 1615

OverviewOverview

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.

About this StructureAbout this Structure

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

ReferenceReference

Structural proteomics of an archaeon., Christendat D, Yee A, Dharamsi A, Kluger Y, Savchenko A, Cort JR, Booth V, Mackereth CD, Saridakis V, Ekiel I, Kozlov G, Maxwell KL, Wu N, McIntosh LP, Gehring K, Kennedy MA, Davidson AR, Pai EF, Gerstein M, Edwards AM, Arrowsmith CH, Nat Struct Biol. 2000 Oct;7(10):903-9. PMID:11017201

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