1rxq
YfiT from Bacillus subtilis is a probable metal-dependent hydrolase with an unusual four-helix bundle topologyYfiT from Bacillus subtilis is a probable metal-dependent hydrolase with an unusual four-helix bundle topology
Structural highlights
FunctionYFIT_BACSU Possible metal-dependent hydrolase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedYfiT, 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. YfiT from Bacillus subtilis is a probable metal-dependent hydrolase with an unusual four-helix bundle topology.,Rajan SS, Yang X, Shuvalova L, Collart F, Anderson WF Biochemistry. 2004 Dec 14;43(49):15472-9. PMID:15581359[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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