PDBsum entry 2fea

Hydrolase

PDB id: 2fea

Contents

Protein chains

226 a.a. *

Ligands

EDO ×10

Metals

_MG ×2

_ZN ×2

Waters ×365

* Residue conservation analysis

PDB id:

2fea

Name:

Hydrolase

Title:

Crystal structure of mtnx phosphatase from bacillus subtilis at 2.00 a resolution

Structure:

2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase. Chain: a, b. Synonym: hk-mtpenyl-1-p phosphatase. Engineered: yes

Source:

Bacillus subtilis. Organism_taxid: 1423. Gene: mtnx. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biol. unit:

Dimer (from PQS)

Resolution:

2.00Å R-factor: 0.163 R-free: 0.217

Authors:

Joint Center For Structural Genomics (Jcsg)

Key ref:

Q.Xu et al. (2007). Crystal structure of MtnX phosphatase from Bacillus subtilis at 2.0 angstroms resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate. Proteins, 69, 433-439. PubMed id: 17654724 DOI: 10.1002/prot.21602

Date:

15-Dec-05 Release date: 27-Dec-05

Protein chains

O31667  (MTNX_BACSU) -  2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase from Bacillus subtilis (strain 168)

Seq: 235 a.a.

Struc: 226 a.a.

Enzyme reactions

• Enzyme class: E.C.3.1.3.87 - 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase.
• Reaction: 2-hydroxy-5-methylsulfanyl-3-oxopent-1-enyl phosphate + H2O = 1,2- dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate

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

Key reference

DOI no: 10.1002/prot.21602

Proteins 69:433-439 (2007)

PubMed id: 17654724

Crystal structure of MtnX phosphatase from Bacillus subtilis at 2.0 angstroms resolution provides a structural basis for bipartite phosphomonoester hydrolysis of 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate.

Q.Xu, K.S.Saikatendu, S.S.Krishna, D.McMullan, P.Abdubek, S.Agarwalla, E.Ambing, T.Astakhova, H.L.Axelrod, D.Carlton, H.J.Chiu, T.Clayton, M.DiDonato, L.Duan, M.A.Elsliger, J.Feuerhelm, S.K.Grzechnik, J.Hale, E.Hampton, G.W.Han, J.Haugen, L.Jaroszewski, K.K.Jin, H.E.Klock, M.W.Knuth, E.Koesema, M.D.Miller, A.T.Morse, E.Nigoghossian, L.Okach, S.Oommachen, J.Paulsen, R.Reyes, C.L.Rife, R.Schwarzenbacher, H.van den Bedem, A.White, G.Wolf, K.O.Hodgson, J.Wooley, A.M.Deacon, A.Godzik, S.A.Lesley, I.A.Wilson.

ABSTRACT

No abstract given.

Selected figure(s)

Figure 1.
Figure 1. Crystal structure of bsmtnX: (A) A simplified schematic of the methionine salvage pathway in B. subtilis according to the schema proposed by Sekowska et al.[2] (B) Stereo ribbon diagram of the bsmtnX monomer color-coded from N-terminus (blue) to C-terminus (red). Helices (H1-H12) and -strands 1- 7) are labeled. (C) Diagram showing the secondary structural elements in bsmtnX superimposed on its primary sequence. The helices, -strands, -turns, and -turns are indicated. The -hairpin is depicted as a red loop. (D) Grasp figure showing distribution of surface electrostatic potential (red-negative (-6kT), blue-positive (+6kT), and white-neutral, where k is the Boltzmann constant and T is the temperature) for bsmtnX positioned in an orientation similar to that in (B). The bound Mg^2+ ion is shown as a green sphere and the position of the buried Zn^2+ ion is indicated by a shaded sphere.

Figure 2.
Figure 2. (A) Structural superposition of bsmtnX (green), mjPSP (PDB: 1l7p; yellow), and paThrH (PDB: 1rku; grey). The active site aspartate, the bound phosphoserine in mjPSP, and the metal ions are shown in ball-and-stick representation. The zinc-binding sub-domain unique to bsmtnX is colored red and an arrow indicates its position. The loop connecting helices H2 and H3, which modulates transition between open/closed states, is also colored red. (B) Structural superposition of the active site residues of the three enzymes. Carbon atoms are colored as in (A), oxygens are red, nitrogens are blue, and phosphate is orange.

The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2007, 69, 433-439) copyright 2007.