PDBsum entry: 1eoi

Hydrolase

PDB id: 1eoi

Contents

Protein chains

222 a.a. *

Ligands

MOO ×3

Waters ×125

* Residue conservation analysis

PDB id:

1eoi

Name:

Hydrolase

Title:

Crystal structure of acid phosphatase from escherichia blatt complexed with the transition state analog molybdate

Structure:

Acid phosphatase. Chain: a, b, c. Engineered: yes

Source:

Escherichia blattae. Organism_taxid: 563. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Hexamer (from PDB file)

Resolution:

2.40Å R-factor: 0.212 R-free: 0.280

Authors:

K.Ishikawa,Y.Mihara,K.Gondoh,E.Suzuki,Y.Asano

Key ref:

K.Ishikawa et al. (2000). X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate. EMBO J, 19, 2412-2423. PubMed id: 10835340 DOI: 10.1093/emboj/19.11.2412

Date:

23-Mar-00 Release date: 23-Mar-01

Protein chains

Q9S1A6  (Q9S1A6_ESCBL) -  Acid phosphatase

Seq: 249 a.a.

Struc: 222 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.3.2 - Acid phosphatase.
• Reaction: A phosphate monoester + H₂O = an alcohol + phosphate

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Cellular component: membrane (2 terms)
• Biological process: metabolic process (1 term)
• Biochemical function: catalytic activity (3 terms)

reference

DOI no: 10.1093/emboj/19.11.2412

EMBO J 19:2412-2423 (2000)

PubMed id: 10835340

X-ray structures of a novel acid phosphatase from Escherichia blattae and its complex with the transition-state analog molybdate.

K.Ishikawa, Y.Mihara, K.Gondoh, E.Suzuki, Y.Asano.

ABSTRACT

The structure of Escherichia blattae non-specific acid phosphatase (EB-NSAP) has been determined at 1.9 A resolution with a bound sulfate marking the phosphate-binding site. The enzyme is a 150 kDa homohexamer. EB-NSAP shares a conserved sequence motif not only with several lipid phosphatases and the mammalian glucose-6-phosphatases, but also with the vanadium-containing chloroperoxidase (CPO) of Curvularia inaequalis. Comparison of the crystal structures of EB-NSAP and CPO reveals striking similarity in the active site structures. In addition, the topology of the EB-NSAP core shows considerable similarity to the fold of the active site containing part of the monomeric 67 kDa CPO, despite the lack of further sequence identity. These two enzymes are apparently related by divergent evolution. We have also determined the crystal structure of EB-NSAP complexed with the transition-state analog molybdate. Structural comparison of the native enzyme and the enzyme-molybdate complex reveals that the side-chain of His150, a putative catalytic residue, moves toward the molybdate so that it forms a hydrogen bond with the metal oxyanion when the molybdenum forms a covalent bond with NE2 of His189.

Selected figure(s)

Figure 5.
Figure 5 Two orthogonal views of the EB-NSAP hexamer viewed (A) along a 3-fold axis and (B) along a 2-fold axis. Ball-and-stick drawings at the center of (A) represent Ile40 and Leu43, which play important roles in assembling the six subunits. This figure was prepared using MOLSCRIPT (Kraulis, 1993) and RASTER3D (Merritt and Murphy, 1994).

Figure 7.
Figure 7 Stereo views of the active site structure. Hydrogen bonds are shown as dashed lines. Sulfur, oxygen, nitrogen, molybdate and vanadium are colored yellow, magenta, cyan, green and orange, respectively. (A) Native EB-NSAP; (B) EB-NSAP complexed with molybdate; (C) apo-CPO; (D) holo-CPO.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2000, 19, 2412-2423) copyright 2000.

Figures were selected by an automated process.