1eje: Difference between revisions

Revision as of 13:28, 21 February 2008

CRYSTAL STRUCTURE OF AN FMN-BINDING PROTEIN

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

1EJE is a Single protein structure of sequence from Methanothermobacter thermautotrophicus with , and as ligands. 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

Page seeded by OCA on Thu Feb 21 12:28:21 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1eje.gif|left|200px]]<br /><applet load="1eje" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1eje.gif|left|200px]]<br /><applet load="1eje" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1eje, resolution 2.20&Aring;" />
 '''CRYSTAL STRUCTURE OF AN FMN-BINDING PROTEIN'''<br />
 ==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==
-EJE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with NI, SO4 and FMN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1EJE OCA].
+EJE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus] with <scene name='pdbligand=NI:'>NI</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EJE OCA].
 ==Reference==
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 [[Category: Bochkarev, A.]]
 [[Category: Christendat, D.]]
-[[Category: Edwards, A.M.]]
+[[Category: Edwards, A M.]]
-[[Category: NESG, Northeast.Structural.Genomics.Consortium.]]
+[[Category: NESG, Northeast Structural Genomics Consortium.]]
 [[Category: Saridakis, V.]]
 [[Category: FMN]]
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 [[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:03:16 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:21 2008''