1rlm: Difference between revisions
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'''Crystal Structure of ybiV from Escherichia coli K12''' | {{Structure | ||
|PDB= 1rlm |SIZE=350|CAPTION= <scene name='initialview01'>1rlm</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | |||
|ACTIVITY= | |||
|GENE= YBIV, B0822 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Crystal Structure of ybiV from Escherichia coli K12''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1RLM is a [ | 1RLM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RLM OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15657928 15657928] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rossman fold]] | [[Category: rossman fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:53:17 2008'' | ||
Revision as of 14:53, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | and | ||||||
| Gene: | YBIV, B0822 (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of ybiV from Escherichia coli K12
OverviewOverview
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 StructureAbout this Structure
1RLM is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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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