Abstract
The protein databases contain many proteins with unknown function. A computational approach for predicting ligand specificity that requires only the sequence of the unknown protein would be valuable for directing experiment-based assignment of function. We focused on a family of unknown proteins in the mechanistically diverse enolase superfamily and used two approaches to assign function: (i) enzymatic assays using libraries of potential substrates, and (ii) in silico docking of the same libraries using a homology model based on the most similar (35% sequence identity) characterized protein. The results matched closely; an experimentally determined structure confirmed the predicted structure of the substrate-liganded complex. We assigned the N-succinyl arginine/lysine racemase function to the family, correcting the annotation (L-Ala-D/L-Glu epimerase) based on the function of the most similar characterized homolog. These studies establish that ligand docking to a homology model can facilitate functional assignment of unknown proteins by restricting the identities of the possible substrates that must be experimentally tested.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Amino Acid Isomerases / chemistry*
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Bacillus / metabolism
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Bacillus cereus / metabolism
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Binding Sites
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Escherichia coli / metabolism
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Mass Spectrometry
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Models, Chemical
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Models, Molecular
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Molecular Sequence Data
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Protein Conformation
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Racemases and Epimerases / chemistry
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Software
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Spectrometry, Mass, Electrospray Ionization
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Substrate Specificity
Substances
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Racemases and Epimerases
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Amino Acid Isomerases
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lysine racemase
Associated data
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PDB/1TKK
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PDB/2P88
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PDB/2P8B
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PDB/2P8C
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PIR/24769846
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PubChem-Substance/24769847
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PubChem-Substance/24769848
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PubChem-Substance/24769849
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PubChem-Substance/24769850
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PubChem-Substance/24769851
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PubChem-Substance/24769852
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PubChem-Substance/24769853
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PubChem-Substance/24769854
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PubChem-Substance/24769855
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PubChem-Substance/24769856
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PubChem-Substance/24769857
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PubChem-Substance/24769858
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PubChem-Substance/24769859
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PubChem-Substance/24769860
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PubChem-Substance/24769861
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PubChem-Substance/24769862
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PubChem-Substance/24769863
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PubChem-Substance/24769864
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PubChem-Substance/24769865
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PubChem-Substance/24769866
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PubChem-Substance/24769867
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PubChem-Substance/24769868
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PubChem-Substance/24769869
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PubChem-Substance/24769870
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PubChem-Substance/24769871
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PubChem-Substance/24769872
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PubChem-Substance/24769873
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PubChem-Substance/24769874
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PubChem-Substance/24769875
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PubChem-Substance/24769876
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PubChem-Substance/24769877
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PubChem-Substance/24769878