1m33
From Proteopedia
(New page: 200px<br /><applet load="1m33" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m33, resolution 1.70Å" /> '''Crystal Structure of...) |
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| - | [[Image:1m33.gif|left|200px]]<br /><applet load="1m33" size=" | + | [[Image:1m33.gif|left|200px]]<br /><applet load="1m33" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1m33, resolution 1.70Å" /> | caption="1m33, resolution 1.70Å" /> | ||
'''Crystal Structure of BioH at 1.7 A'''<br /> | '''Crystal Structure of BioH at 1.7 A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Structural proteomics projects are generating three-dimensional structures | + | Structural proteomics projects are generating three-dimensional structures of novel, uncharacterized proteins at an increasing rate. However, structure alone is often insufficient to deduce the specific biochemical function of a protein. Here we determined the function for a protein using a strategy that integrates structural and bioinformatics data with parallel experimental screening for enzymatic activity. BioH is involved in biotin biosynthesis in Escherichia coli and had no previously known biochemical function. The crystal structure of BioH was determined at 1.7 A resolution. An automated procedure was used to compare the structure of BioH with structural templates from a variety of different enzyme active sites. This screen identified a catalytic triad (Ser82, His235, and Asp207) with a configuration similar to that of the catalytic triad of hydrolases. Analysis of BioH with a panel of hydrolase assays revealed a carboxylesterase activity with a preference for short acyl chain substrates. The combined use of structural bioinformatics with experimental screens for detecting enzyme activity could greatly enhance the rate at which function is determined from structure. |
==About this Structure== | ==About this Structure== | ||
| - | 1M33 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with 3OH and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1M33 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=3OH:'>3OH</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M33 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Edwards, A.]] | [[Category: Edwards, A.]] | ||
[[Category: Joachimiak, A.]] | [[Category: Joachimiak, A.]] | ||
| - | [[Category: MCSG, Midwest | + | [[Category: MCSG, Midwest Center for Structural Genomics.]] |
[[Category: Sanishvili, R.]] | [[Category: Sanishvili, R.]] | ||
[[Category: Savchenko, A.]] | [[Category: Savchenko, A.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:50:57 2008'' |
Revision as of 11:50, 21 February 2008
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Crystal Structure of BioH at 1.7 A
Overview
Structural proteomics projects are generating three-dimensional structures of novel, uncharacterized proteins at an increasing rate. However, structure alone is often insufficient to deduce the specific biochemical function of a protein. Here we determined the function for a protein using a strategy that integrates structural and bioinformatics data with parallel experimental screening for enzymatic activity. BioH is involved in biotin biosynthesis in Escherichia coli and had no previously known biochemical function. The crystal structure of BioH was determined at 1.7 A resolution. An automated procedure was used to compare the structure of BioH with structural templates from a variety of different enzyme active sites. This screen identified a catalytic triad (Ser82, His235, and Asp207) with a configuration similar to that of the catalytic triad of hydrolases. Analysis of BioH with a panel of hydrolase assays revealed a carboxylesterase activity with a preference for short acyl chain substrates. The combined use of structural bioinformatics with experimental screens for detecting enzyme activity could greatly enhance the rate at which function is determined from structure.
About this Structure
1M33 is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
Integrating structure, bioinformatics, and enzymology to discover function: BioH, a new carboxylesterase from Escherichia coli., Sanishvili R, Yakunin AF, Laskowski RA, Skarina T, Evdokimova E, Doherty-Kirby A, Lajoie GA, Thornton JM, Arrowsmith CH, Savchenko A, Joachimiak A, Edwards AM, J Biol Chem. 2003 Jul 11;278(28):26039-45. Epub 2003 May 5. PMID:12732651
Page seeded by OCA on Thu Feb 21 13:50:57 2008
Categories: Escherichia coli | Single protein | Edwards, A. | Joachimiak, A. | MCSG, Midwest Center for Structural Genomics. | Sanishvili, R. | Savchenko, A. | Skarina, T. | Yakunin, A. | 3OH | EDO | Alpha-betta-alpha sandwich | Mcsg | Midwest center for structural genomics | Protein structure initiative | Psi | Structural genomics
