1gh9

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Revision as of 16:56, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1gh9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gh9" /> '''SOLUTION STRUCTURE OF A 8.3 KDA PROTEIN (GEN...)
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1gh9

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SOLUTION STRUCTURE OF A 8.3 KDA PROTEIN (GENE MTH1184) FROM METHANOBACTERIUM THERMOAUTOTROPHICUM

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

1GH9 is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. This structure superseeds the now removed PDB entry 1DW7. 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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