1RXQ

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

1RXQ の概要

• エントリーDOI: 10.2210/pdb1rxq/pdb
• 分子名称: yfiT, NICKEL (II) ION, GLUTAMIC ACID, ... (8 entities in total)
• 機能のキーワード: nickel-binding, hydrolase, helix-bundle, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, metal-binding protein, metal binding protein
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 84419.31

構造登録者

Rajan, S.S.,Yang, X.,Anderson, W.F.,Midwest Center for Structural Genomics (MCSG) (登録日: 2003-12-18, 公開日: 2004-07-20, 最終更新日: 2024-10-16)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.7 Å)