1kq4: Difference between revisions

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New page: left|200px<br /><applet load="1kq4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kq4, resolution 2.25Å" /> '''Crystal Structure of...
 
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[[Image:1kq4.gif|left|200px]]<br /><applet load="1kq4" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1kq4.gif|left|200px]]<br /><applet load="1kq4" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1kq4, resolution 2.25&Aring;" />
caption="1kq4, resolution 2.25&Aring;" />
'''Crystal Structure of Thy1-Complementing Protein (TM0449) from Thermotoga maritima at 2.25 A Resolution'''<br />
'''Crystal Structure of Thy1-Complementing Protein (TM0449) from Thermotoga maritima at 2.25 A Resolution'''<br />


==Overview==
==Overview==
Structural genomics is emerging as a principal approach to define protein, structure-function relationships. To apply this approach on a genomic, scale, novel methods and technologies must be developed to determine large, numbers of structures. We describe the design and implementation of a, high-throughput structural genomics pipeline and its application to the, proteome of the thermophilic bacterium Thermotoga maritima. By using this, pipeline, we successfully cloned and attempted expression of 1,376 of the, predicted 1,877 genes (73%) and have identified crystallization conditions, for 432 proteins, comprising 23% of the T. maritima proteome., Representative structures from TM0423 glycerol dehydrogenase and TM0449, thymidylate synthase-complementing protein are presented as examples of, final outputs from the pipeline.
Structural genomics is emerging as a principal approach to define protein structure-function relationships. To apply this approach on a genomic scale, novel methods and technologies must be developed to determine large numbers of structures. We describe the design and implementation of a high-throughput structural genomics pipeline and its application to the proteome of the thermophilic bacterium Thermotoga maritima. By using this pipeline, we successfully cloned and attempted expression of 1,376 of the predicted 1,877 genes (73%) and have identified crystallization conditions for 432 proteins, comprising 23% of the T. maritima proteome. Representative structures from TM0423 glycerol dehydrogenase and TM0449 thymidylate synthase-complementing protein are presented as examples of final outputs from the pipeline.


==About this Structure==
==About this Structure==
1KQ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KQ4 OCA].  
1KQ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KQ4 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
[[Category: JCSG, Joint.Center.for.Structural.Genomics.]]
[[Category: JCSG, Joint Center for Structural Genomics.]]
[[Category: Miller, M.D.]]
[[Category: Miller, M D.]]
[[Category: Wilson, I.A.]]
[[Category: Wilson, I A.]]
[[Category: FAD]]
[[Category: FAD]]
[[Category: flavin-adenine dinucleotide]]
[[Category: flavin-adenine dinucleotide]]
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[[Category: thy1-complementing protein from thermotoga maritima]]
[[Category: thy1-complementing protein from thermotoga maritima]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:36:57 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:45 2008''

Revision as of 14:36, 21 February 2008

File:1kq4.gif


1kq4, resolution 2.25Å

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Crystal Structure of Thy1-Complementing Protein (TM0449) from Thermotoga maritima at 2.25 A Resolution

OverviewOverview

Structural genomics is emerging as a principal approach to define protein structure-function relationships. To apply this approach on a genomic scale, novel methods and technologies must be developed to determine large numbers of structures. We describe the design and implementation of a high-throughput structural genomics pipeline and its application to the proteome of the thermophilic bacterium Thermotoga maritima. By using this pipeline, we successfully cloned and attempted expression of 1,376 of the predicted 1,877 genes (73%) and have identified crystallization conditions for 432 proteins, comprising 23% of the T. maritima proteome. Representative structures from TM0423 glycerol dehydrogenase and TM0449 thymidylate synthase-complementing protein are presented as examples of final outputs from the pipeline.

About this StructureAbout this Structure

1KQ4 is a Single protein structure of sequence from Thermotoga maritima with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structural genomics of the Thermotoga maritima proteome implemented in a high-throughput structure determination pipeline., Lesley SA, Kuhn P, Godzik A, Deacon AM, Mathews I, Kreusch A, Spraggon G, Klock HE, McMullan D, Shin T, Vincent J, Robb A, Brinen LS, Miller MD, McPhillips TM, Miller MA, Scheibe D, Canaves JM, Guda C, Jaroszewski L, Selby TL, Elsliger MA, Wooley J, Taylor SS, Hodgson KO, Wilson IA, Schultz PG, Stevens RC, Proc Natl Acad Sci U S A. 2002 Sep 3;99(18):11664-9. Epub 2002 Aug 22. PMID:12193646

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