1RXQ

YfiT from Bacillus subtilis is a probable metal-dependent hydrolase with an unusual four-helix bundle topology

Summary for 1RXQ

• Entry DOI: 10.2210/pdb1rxq/pdb
• Descriptor: yfiT, NICKEL (II) ION, GLUTAMIC ACID, ... (8 entities in total)
• Functional Keywords: nickel-binding, hydrolase, helix-bundle, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, metal-binding protein, metal binding protein
• Biological source: Bacillus subtilis
• Total number of polymer chains: 4
• Total formula weight: 84419.31

Authors

Rajan, S.S.,Yang, X.,Anderson, W.F.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2003-12-18, release date: 2004-07-20, Last modification date: 2024-10-16)

Primary citation

Rajan, S.S.,Yang, X.,Shuvalova, L.,Collart, F.,Anderson, W.F.
YfiT from Bacillus subtilis Is a Probable Metal-Dependent Hydrolase with an Unusual Four-Helix Bundle Topology
Biochemistry, 43:15472-15479, 2004

PubMed Abstract: 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.

PubMed: 15581359
DOI: 10.1021/bi048665r

Experimental method

X-RAY DIFFRACTION (1.7 Å)