PDBsum entry 1std

Lyase (carbon-oxygen)

PDB id: 1std

Contents

Protein chain

162 a.a. *

Ligands

SO4

BFS

Waters ×4

* Residue conservation analysis

PDB id:

1std

Name:

Lyase (carbon-oxygen)

Title:

Crystal structure of scytalone dehydratase: a disease determinant of the rice pathogen, magnaporthe grisea

Structure:

Scytalone dehydratase. Chain: a. Engineered: yes

Source:

Magnaporthe grisea. Organism_taxid: 148305

Biol. unit:

Trimer (from PQS)

Resolution:

2.90Å R-factor: 0.179

Authors:

T.Lundqvist,Y.Lindqvist

Key ref:

T.Lundqvist et al. (1994). Crystal structure of scytalone dehydratase--a disease determinant of the rice pathogen, Magnaporthe grisea. Structure, 2, 937-944. PubMed id: 7866745 DOI: 10.1016/S0969-2126(94)00095-6

Date:

19-Aug-94 Release date: 19-Aug-95

Protein chain

P56221  (SCYD_MAGO7) -  Scytalone dehydratase from Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)

Seq: 172 a.a.

Struc: 162 a.a.

Enzyme reactions

• Enzyme class: E.C.4.2.1.94 - scytalone dehydratase.
• Reaction: scytalone = 1,3,8-trihydroxynaphthalene + H2O

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

Added reference

DOI no: 10.1016/S0969-2126(94)00095-6

Structure 2:937-944 (1994)

PubMed id: 7866745

Crystal structure of scytalone dehydratase--a disease determinant of the rice pathogen, Magnaporthe grisea.

T.Lundqvist, J.Rice, C.N.Hodge, G.S.Basarab, J.Pierce, Y.Lindqvist.

ABSTRACT

BACKGROUND: Rice blast is caused by the pathogenic fungus,-Magnaporthe grisea. Non-pathogenic mutants have been identified that lack enzymes in the biosynthetic pathway of dihydroxynapthalene-derived melanin. These enzymes are therefore prime targets for fungicides designed to control rice blast disease. One of the enzymes identified by genetic analysis as a disease determinant is scytalone dehydratase. RESULTS: The three-dimensional structure of scytalone dehydratase in complex with a competitive inhibitor has been determined at 2.9 A resolution. A novel fold, a cone-shaped alpha + beta barrel, is adopted by the monomer in this trimeric protein, burying the hydrophobic active site in its interior. The interactions of the inhibitor with the protein side chains have been identified. The similarity of the inhibitor to the substrate and the side chains involved in binding afford some insights into possible catalytic mechanisms. CONCLUSIONS: These results provide a first look into the structure and catalytic residues of a non-metal dehydratase, a large class of hitherto structurally uncharacterized enzymes. It is envisaged that a detailed structural description of scytalone dehydratase will assist in the design of new inhibitors for controlling rice blast disease.

Selected figure(s)

Figure 1.
Figure 1. (a) Reactions catalyzed by scytalone dehydratase. Conversion of scytalone (1) to 1,3,8-trihydroxynaphthalene (2); conversion of vermelone (3) to 1,8-dihydroxynapthalene (4); conversion of an artificial substrate (5) to an α ,β-unsaturated ketone (6). (b) Structure of salicylamide inhibitors; (R)-(+)-N-[1- (4-bromophenyl)ethyl]-5-fluorosalicylamide (7),N-(3,3-diphenylpropyl)-5-fluorosalicylamide (8) and (R)-(+)-N-[1-(4-iodophenyl)ethyl]-5-fluorosalicylamide (9). Figure 1. (a) Reactions catalyzed by scytalone dehydratase. Conversion of scytalone (1) to 1,3,8-trihydroxynaphthalene (2); conversion of vermelone (3) to 1,8-dihydroxynapthalene (4); conversion of an artificial substrate (5) to an α ,β-unsaturated ketone (6). (b) Structure of salicylamide inhibitors; (R)-(+)-N-[1- (4-bromophenyl)ethyl]-5-fluorosalicylamide (7),N-(3,3-diphenylpropyl)-5-fluorosalicylamide (8) and (R)-(+)-N-[1-(4-iodophenyl)ethyl]-5-fluorosalicylamide (9).

Figure 10.
Figure 10. Reaction mechanism based on a model where the substrate has been positioned in the active site so as to overlap with the analogous parts of the inhibitor. Figure 10. Reaction mechanism based on a model where the substrate has been positioned in the active site so as to overlap with the analogous parts of the inhibitor.

The above figures are reprinted by permission from Cell Press: Structure (1994, 2, 937-944) copyright 1994.

Figures were selected by an automated process.