PDBsum entry 1ba3

Oxidoreductase

PDB id: 1ba3

Contents

Protein chain

540 a.a.

Ligands

MBR ×2

Waters ×353

References listed in PDB file

Key reference

Title

Structural basis for the inhibition of firefly luciferase by a general anesthetic.

Authors

N.P.Franks, A.Jenkins, E.Conti, W.R.Lieb, P.Brick.

Ref.

Biophys J, 1998, 75, 2205-2211.

PubMed id

9788915

Abstract

The firefly luciferase enzyme from Photinus pyralis is probably the best-characterized model system for studying anesthetic-protein interactions. It binds a diverse range of general anesthetics over a large potency range, displays a sensitivity to anesthetics that is very similar to that found in animals, and has an anesthetic sensitivity that can be modulated by one of its substrates (ATP). In this paper we describe the properties of bromoform acting as a general anesthetic (in Rana temporaria tadpoles) and as an inhibitor of the firefly luciferase enzyme at high and low ATP concentrations. In addition, we describe the crystal structure of the low-ATP form of the luciferase enzyme in the presence of bromoform at 2.2-A resolution. These results provide a structural basis for understanding the anesthetic inhibition of the enzyme, as well as an explanation for the ATP modulation of its anesthetic sensitivity.

Secondary reference #1

Title

Structural basis for the activation of phenylalanine in the non-Ribosomal biosynthesis of gramicidin s.

Authors

E.Conti, T.Stachelhaus, M.A.Marahiel, P.Brick.

Ref.

Embo J, 1997, 16, 4174-4183. [DOI no: 10.1093/emboj/16.14.4174]

PubMed id

9250661

Figure 2.
Figure 2 Stereo diagram of the large N-terminal domain of PheA showing the bound ligands coloured as in Figure 1. The -sheet A is on the left-hand side, -sheet B is on the right-hand side, and the -barrel is at the top of the figure. The N-terminus of the protein is at the top of the figure. The disordered loop (residues 192 -196) near the active site is coloured violet.

Figure 6.
Figure 6 Schematic representation of the hydrogen bonding between PheA and the phenylalanine and AMP ligands.

The above figures are reproduced from the cited reference which is an Open Access publication published by Macmillan Publishers Ltd

Secondary reference #2

Title

Crystal structure of firefly luciferase throws light on a superfamily of adenylate-Forming enzymes.

Authors

E.Conti, N.P.Franks, P.Brick.

Ref.

Structure, 1996, 4, 287-298. [DOI no: 10.1016/S0969-2126(96)00033-0]

PubMed id

8805533

Figure 2.
Figure 2. Ribbon representations of the firefly luciferase molecule shown in two orthogonal views. The three subdomains of the large N-terminal domain are shown in blue (β-sheet A), purple (β-sheet B) and green (β-barrel) and the small C-terminal domain is shown in yellow. Disordered loops are drawn in violet. Figure 2. Ribbon representations of the firefly luciferase molecule shown in two orthogonal views. The three subdomains of the large N-terminal domain are shown in blue (β-sheet A), purple (β-sheet B) and green (β-barrel) and the small C-terminal domain is shown in yellow. Disordered loops are drawn in violet. (Generated using the program MOLSCRIPT [[4]62].)

Figure 3.
Figure 3. Stereo α-carbon trace viewed in a similar orientation to Figure 2a, with some sequence numbering for reference. Figure 3. Stereo α-carbon trace viewed in a similar orientation to [3]Figure 2a, with some sequence numbering for reference.

The above figures are reproduced from the cited reference with permission from Cell Press

Secondary reference #3

Title

Crystallization and preliminary diffraction studies of firefly luciferase from photinus pyralis.

Authors

E.Conti, L.F.Lloyd, J.Akins, N.P.Franks, P.Brick.

Ref.

Acta Crystallogr D Biol Crystallogr, 1996, 52, 876-878. [DOI no: 10.1107/S0907444996002405]

PubMed id

15299657

Figure 1.
Fig. 1. Tetragonal crystals of firefly luciferase with a cross-section up to 0.06 mm, which have been grown by the microbatch technique under oil.

The above figure is reproduced from the cited reference with permission from the IUCr