|Biochemistry (2004) 43(49):15472-9|
|Midwest Center for Structural Genomics|
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YfiT, a 19-kDa polypeptide from Bacillus subtilis, belongs to a small sequence family with members predominantly from Gram positive bacteria. ...
We have determined the crystal structure of YfiT in complex with Ni(2+) to a resolution of 1.7 A. YfiT exists as a dimer and binds Ni(2+) in a 1:1 stoichiometry. The protein has an unusual four-helix bundle topology and coordinates Ni(2+) in an octahedral geometry with three conserved histidines and three waters. Although there is no similarity in their overall structures, the coordination geometry of the metal and the residues that constitute the putative active site in YfiT are similar to those of metalloproteases such as thermolysin. Our structural analyses suggest that YfiT might function as a metal-dependent hydrolase.
|enzymology genetics metabolism chemistry |
|Crystallography, X-Ray Bacillus subtilis Dimerization Nickel Sequence Alignment Metalloproteins Hydrolases Thermolysin Genome, Bacterial Binding Sites Protein Structure, Secondary Sequence Homology, Amino Acid Bacterial Proteins Structural Homology, Protein |
|14 (Last update: 05/23/2018 7:10:32pm)|
|Biochemistry. 2004 Dec 14;43(49):15472-9.|