1VPR

Crystal structure of a luciferase domain from the dinoflagellate Lingulodinium polyedrum

Summary for 1VPR

• Entry DOI: 10.2210/pdb1vpr/pdb
• Descriptor: luciferase (2 entities in total)
• Functional Keywords: beta barrel, fatty acid binding protein, lipocalin, luciferase, ph regulation, luminescent protein
• Biological source: Lingulodinium polyedrum
• Total number of polymer chains: 1
• Total formula weight: 42025.52

Authors

Schultz, L.W.,Liu, L.,Cegielski, M.,Hastings, J.W. (deposition date: 2004-11-15, release date: 2005-02-08, Last modification date: 2024-10-30)

Primary citation

Schultz, L.W.,Liu, L.,Cegielski, M.,Hastings, J.W.
Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole
Proc.Natl.Acad.Sci.USA, 102:1378-1383, 2005

PubMed Abstract: The luciferase of Lingulodinium polyedrum, a marine bioluminescent dinoflagellate, consists of three similar but not identical domains in a single polypeptide. Each encodes an active luciferase that catalyzes the oxidation of a chlorophyll-derived open tetrapyrrole (dinoflagellate luciferin) to produce blue light. These domains share no sequence similarity with any other in the GenBank database and no structural or motif similarity with any other luciferase. We report here the 1.8-A crystal structure of the third domain, D3, at pH 8, and a mechanism for its activity regulation by pH. D3 consists of two major structural elements: a beta-barrel pocket putatively for substrate binding and catalysis and a regulatory three-helix bundle. N-terminal histidine residues previously shown to regulate activity by pH are at the interface of the helices in the bundle. Molecular dynamics calculations indicate that, in response to changes in pH, these histidines could trigger a large molecular motion of the bundle, thereby exposing the active site to the substrate.

PubMed: 15665092
DOI: 10.1073/pnas.0409335102

Experimental method

X-RAY DIFFRACTION (1.8 Å)