PDBsum entry 2fwm

Oxidoreductase

PDB id: 2fwm

Contents

Protein chain

212 a.a. *

Waters ×109

* Residue conservation analysis

PDB id:

2fwm

Name:

Oxidoreductase

Title:

Crystal structure of e. Coli enta, a 2,3-dihydrodihydroxy benzoate dehydrogenase

Structure:

2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase. Chain: x. Engineered: yes

Source:

Escherichia coli. Organism_taxid: 562. Strain: jm109. Gene: enta. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Biol. unit:

Tetramer (from PDB file)

Resolution:

2.00Å R-factor: 0.186 R-free: 0.214

Authors:

A.M.Gulick,W.L.Duax

Key ref:

J.A.Sundlov et al. (2006). Determination of the crystal structure of EntA, a 2,3-dihydro-2,3-dihydroxybenzoic acid dehydrogenase from Escherichia coli. Acta Crystallogr D Biol Crystallogr, 62, 734-740. PubMed id: 16790929 DOI: 10.1107/S0907444906015824

Date:

02-Feb-06 Release date: 27-Jun-06

Protein chain

P15047  (ENTA_ECOLI) -  2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase from Escherichia coli (strain K12)

Seq: 248 a.a.

Struc: 212 a.a.

Enzyme reactions

• Enzyme class: E.C.1.3.1.28 - 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase.
• Reaction: (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate + NAD⁺ = 2,3- dihydroxybenzoate + NADH + H⁺

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

reference

DOI no: 10.1107/S0907444906015824

Acta Crystallogr D Biol Crystallogr 62:734-740 (2006)

PubMed id: 16790929

Determination of the crystal structure of EntA, a 2,3-dihydro-2,3-dihydroxybenzoic acid dehydrogenase from Escherichia coli.

J.A.Sundlov, J.A.Garringer, J.M.Carney, A.S.Reger, E.J.Drake, W.L.Duax, A.M.Gulick.

ABSTRACT

The Escherichia coli enterobactin synthetic cluster is composed of six proteins, EntA-EntF, that form the enterobactin molecule from three serine molecules and three molecules of 2,3-dihydroxybenzoic acid (DHB). EntC, EntB and EntA catalyze the three-step synthesis of DHB from chorismate. EntA is a member of the short-chain oxidoreductase (SCOR) family of proteins and catalyzes the final step in DHB synthesis, the NAD+-dependent oxidation of 2,3-dihydro-2,3-dihydroxybenzoic acid to DHB. The structure of EntA has been determined by multi-wavelength anomalous dispersion methods. Here, the 2.0 A crystal structure of EntA in the unliganded form is presented. Analysis of the structure in light of recent structural and bioinformatic analysis of other members of the SCOR family provides insight into the residues involved in cofactor and substrate binding.

Selected figure(s)

Figure 3.
Figure 3 Structure of the EntA monomer and tetramer. (a) Ribbon diagram of the EntA monomer. The central -sheet is shown in red, while the surrounding helices are shown in blue. The secondary-structural elements are labeled. Note that helices 1 and 3 are not present in the EntA structure; in accordance with secondary-structure nomenclature for prior SCOR proteins (Duax et al., 2000[Duax, W. L., Ghosh, D. & Pletnev, V. (2000). Vitam. Horm. 58, 121-148.]), the helices are labeled 2, 4, 5, 6, and 7. (b) The EntA tetramer is shown viewed down one twofold axis of 222 crystallographic symmetry. The two top and two bottom subunits interact around the four-helix bundle formed by helices 5 and 6. The C-terminal loops and 7 form interactions between dimers.

Figure 4.
Figure 4 Proposed substrate-binding pocket of EntA. The residues of the EntA protein predicted by covariance analysis to contribute to 2,3-DHDHB-specific binding are labeled. The cofactor molecule (shown in orange) was modeled into the unliganded EntA structure by superimposing the 7 -hydroxysteroid dehydrogenase (PDB code 1fmc ) structure onto the EntA molecule.

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 734-740) copyright 2006.

Figures were selected by the author.