1uxo
From Proteopedia
(New page: 200px<br /><applet load="1uxo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uxo, resolution 1.80Å" /> '''THE CRYSTAL STRUCTUR...) |
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| - | [[Image:1uxo.gif|left|200px]]<br /><applet load="1uxo" size=" | + | [[Image:1uxo.gif|left|200px]]<br /><applet load="1uxo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1uxo, resolution 1.80Å" /> | caption="1uxo, resolution 1.80Å" /> | ||
'''THE CRYSTAL STRUCTURE OF THE YDEN GENE PRODUCT FROM B. SUBTILIS'''<br /> | '''THE CRYSTAL STRUCTURE OF THE YDEN GENE PRODUCT FROM B. SUBTILIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | High-throughput (HT) protein crystallography is severely impeded by the | + | High-throughput (HT) protein crystallography is severely impeded by the relatively low success rate of protein crystallization. Proteins whose structures are not solved in the HT pipeline owing to attrition in any phase of the project are referred to as the high-hanging fruit, in contrast to those proteins that yielded good-quality crystals and crystal structures, which are referred to as low-hanging fruit. It has previously been shown that proteins that do not crystallize in the wild-type form can have their surfaces engineered by site-directed mutagenesis in order to create patches of low conformational entropy that are conducive to forming intermolecular interactions. The application of this method to selected proteins from the Bacillus subtilis genome which failed to crystallize in the HT mode is now reported. In this paper, the crystal structure of the product of the YdeN gene is reported. Of three prepared double mutants, i.e. E124A/K127A, E167A/E169A and K88A/Q89A, the latter gave high-quality crystals and the crystal structure was solved by SAD at 1.8 angstroms resolution. The protein is a canonical alpha/beta hydrolase, with an active site that is accessible to solvent. |
==About this Structure== | ==About this Structure== | ||
| - | 1UXO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | + | 1UXO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UXO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Cooper, D.]] | [[Category: Cooper, D.]] | ||
[[Category: Derewenda, U.]] | [[Category: Derewenda, U.]] | ||
| - | [[Category: Derewenda, Z | + | [[Category: Derewenda, Z S.]] |
[[Category: Devedjiev, Y.]] | [[Category: Devedjiev, Y.]] | ||
[[Category: Gabrys, A.]] | [[Category: Gabrys, A.]] | ||
| - | [[Category: Janda, I | + | [[Category: Janda, I K.]] |
[[Category: Joachimiak, A.]] | [[Category: Joachimiak, A.]] | ||
| - | [[Category: MCSG, Midwest | + | [[Category: MCSG, Midwest Center for Structural Genomics.]] |
[[Category: Minor, W.]] | [[Category: Minor, W.]] | ||
[[Category: a/b hydrolase]] | [[Category: a/b hydrolase]] | ||
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[[Category: psi]] | [[Category: psi]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:29:26 2008'' |
Revision as of 13:29, 21 February 2008
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THE CRYSTAL STRUCTURE OF THE YDEN GENE PRODUCT FROM B. SUBTILIS
Overview
High-throughput (HT) protein crystallography is severely impeded by the relatively low success rate of protein crystallization. Proteins whose structures are not solved in the HT pipeline owing to attrition in any phase of the project are referred to as the high-hanging fruit, in contrast to those proteins that yielded good-quality crystals and crystal structures, which are referred to as low-hanging fruit. It has previously been shown that proteins that do not crystallize in the wild-type form can have their surfaces engineered by site-directed mutagenesis in order to create patches of low conformational entropy that are conducive to forming intermolecular interactions. The application of this method to selected proteins from the Bacillus subtilis genome which failed to crystallize in the HT mode is now reported. In this paper, the crystal structure of the product of the YdeN gene is reported. Of three prepared double mutants, i.e. E124A/K127A, E167A/E169A and K88A/Q89A, the latter gave high-quality crystals and the crystal structure was solved by SAD at 1.8 angstroms resolution. The protein is a canonical alpha/beta hydrolase, with an active site that is accessible to solvent.
About this Structure
1UXO is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Harvesting the high-hanging fruit: the structure of the YdeN gene product from Bacillus subtilis at 1.8 angstroms resolution., Janda I, Devedjiev Y, Cooper D, Chruszcz M, Derewenda U, Gabrys A, Minor W, Joachimiak A, Derewenda ZS, Acta Crystallogr D Biol Crystallogr. 2004 Jun;60(Pt 6):1101-7. Epub 2004, May 21. PMID:15159570
Page seeded by OCA on Thu Feb 21 15:29:26 2008
Categories: Bacillus subtilis | Single protein | Chruszcz, M. | Cooper, D. | Derewenda, U. | Derewenda, Z S. | Devedjiev, Y. | Gabrys, A. | Janda, I K. | Joachimiak, A. | MCSG, Midwest Center for Structural Genomics. | Minor, W. | A/b hydrolase | Esterase | Mcsg | Midwest center for structural genomics | Protein structure initiative | Psi
