Title : From structure to function: YrbI from Haemophilus influenzae (HI1679) is a phosphatase - Parsons_2002_Proteins_46_393 |
Author(s) : Parsons JF , Lim K , Tempczyk A , Krajewski W , Eisenstein E , Herzberg O |
Ref : Proteins , 46 :393 , 2002 |
Abstract :
The crystal structure of the YrbI protein from Haemophilus influenzae (HI1679) was determined at a 1.67-A resolution. The function of the protein had not been assigned previously, and it is annotated as hypothetical in sequence databases. The protein exhibits the alpha/beta-hydrolase fold (also termed the Rossmann fold) and resembles most closely the fold of the L-2-haloacid dehalogenase (HAD) superfamily. Following this observation, a detailed sequence analysis revealed remote homology to two members of the HAD superfamily, the P-domain of Ca(2+) ATPase and phosphoserine phosphatase. The 19-kDa chains of HI1679 form a tetramer both in solution and in the crystalline form. The four monomers are arranged in a ring such that four beta-hairpin loops, each inserted after the first beta-strand of the core alpha/beta-fold, form an eight-stranded barrel at the center of the assembly. Four active sites are located at the subunit interfaces. Each active site is occupied by a cobalt ion, a metal used for crystallization. The cobalt is octahedrally coordinated to two aspartate side-chains, a backbone oxygen, and three solvent molecules, indicating that the physiological metal may be magnesium. HI1679 hydrolyzes a number of phosphates, including 6-phosphogluconate and phosphotyrosine, suggesting that it functions as a phosphatase in vivo. The physiological substrate is yet to be identified; however the location of the gene on the yrb operon suggests involvement in sugar metabolism. |
PubMedSearch : Parsons_2002_Proteins_46_393 |
PubMedID: 11835514 |
Parsons JF, Lim K, Tempczyk A, Krajewski W, Eisenstein E, Herzberg O (2002)
From structure to function: YrbI from Haemophilus influenzae (HI1679) is a phosphatase
Proteins
46 :393
Parsons JF, Lim K, Tempczyk A, Krajewski W, Eisenstein E, Herzberg O (2002)
Proteins
46 :393