1rlo
From Proteopedia
(New page: 200px<br /><applet load="1rlo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rlo, resolution 2.00Å" /> '''Phospho-aspartyl Int...) |
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| - | [[Image:1rlo.jpg|left|200px]]<br /><applet load="1rlo" size=" | + | [[Image:1rlo.jpg|left|200px]]<br /><applet load="1rlo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rlo, resolution 2.00Å" /> | caption="1rlo, resolution 2.00Å" /> | ||
'''Phospho-aspartyl Intermediate Analogue of ybiV from E. coli K12'''<br /> | '''Phospho-aspartyl Intermediate Analogue of ybiV from E. coli K12'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The protein YbiV from Escherichia coli K12 MG1655 is a hypothetical | + | The protein YbiV from Escherichia coli K12 MG1655 is a hypothetical protein with sequence homology to the haloacid dehalogenase (HAD) superfamily of proteins. Although numerous members of this family have been identified, the functions of few are known. Using the crystal structure, sequence analysis, and biochemical assays, we have characterized YbiV as a HAD phosphatase. The crystal structure of YbiV reveals a two-domain protein, one with the characteristic HAD hydrolase fold, the other an inserted alpha/beta fold. In an effort to understand the mechanism, we also solved and report the structures of YbiV in complex with beryllofluoride (BeF3-) and aluminum trifluoride (AlF3), which have been shown to mimic the phosphorylated intermediate and transition state for hydrolysis, respectively, in analogy to other HAD phosphatases. Analysis of the structures reveals the substrate-binding cavity, which is hydrophilic in nature. Both structure and sequence homology indicate YbiV may be a sugar phosphatase, which is supported by biochemical assays that measured the release of free phosphate on a number of sugar-like substrates. We also investigated available genomic and functional data in an effort to determine the physiological substrate. |
==About this Structure== | ==About this Structure== | ||
| - | 1RLO 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 MG and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RLO 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=MG:'>MG</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Lee, S | + | [[Category: Lee, S Y.]] |
[[Category: McCullagh, E.]] | [[Category: McCullagh, E.]] | ||
[[Category: Roberts, A.]] | [[Category: Roberts, A.]] | ||
| - | [[Category: Silversmith, R | + | [[Category: Silversmith, R E.]] |
| - | [[Category: Wemmer, D | + | [[Category: Wemmer, D E.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: phospho-aspartate]] | [[Category: phospho-aspartate]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:14 2008'' |
Revision as of 12:52, 21 February 2008
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Phospho-aspartyl Intermediate Analogue of ybiV from E. coli K12
Overview
The protein YbiV from Escherichia coli K12 MG1655 is a hypothetical protein with sequence homology to the haloacid dehalogenase (HAD) superfamily of proteins. Although numerous members of this family have been identified, the functions of few are known. Using the crystal structure, sequence analysis, and biochemical assays, we have characterized YbiV as a HAD phosphatase. The crystal structure of YbiV reveals a two-domain protein, one with the characteristic HAD hydrolase fold, the other an inserted alpha/beta fold. In an effort to understand the mechanism, we also solved and report the structures of YbiV in complex with beryllofluoride (BeF3-) and aluminum trifluoride (AlF3), which have been shown to mimic the phosphorylated intermediate and transition state for hydrolysis, respectively, in analogy to other HAD phosphatases. Analysis of the structures reveals the substrate-binding cavity, which is hydrophilic in nature. Both structure and sequence homology indicate YbiV may be a sugar phosphatase, which is supported by biochemical assays that measured the release of free phosphate on a number of sugar-like substrates. We also investigated available genomic and functional data in an effort to determine the physiological substrate.
About this Structure
1RLO is a Single protein structure of sequence from Escherichia coli with and as ligands. Full crystallographic information is available from OCA.
Reference
YbiV from Escherichia coli K12 is a HAD phosphatase., Roberts A, Lee SY, McCullagh E, Silversmith RE, Wemmer DE, Proteins. 2005 Mar 1;58(4):790-801. PMID:15657928
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