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Three‐dimensional model of the α‐subunit of bacterial luciferase
Author(s) -
Sandalova Tatyana,
Lindqvist Ylva
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340230213
Subject(s) - luciferase , globular protein , protein subunit , protein secondary structure , alpha (finance) , protein structure , chemistry , structural similarity , beta (programming language) , sequence (biology) , biophysics , similarity (geometry) , barrel (horology) , biochemistry , biology , mathematics , materials science , computer science , artificial intelligence , transfection , construct validity , statistics , image (mathematics) , gene , programming language , psychometrics , composite material
The predicted secondary structure of both subunits of bacterial luciferase is in accordance with a regular 8‐fold α/β‐barrel structure. The 3D profile 1,2 confirmed that luciferase subunits are compatible with the α/β‐barrel despite the absence of sequence similarity with any α/β‐barrel protein. The three‐dimensional structure of 260 residues of the α‐chain of luciferase was modeled from coordinates of glycolate oxidase and then energy minimized. The model obtained satisfies the criteria for the structure of a globular protein and is in accordance with known experimental data. From the model it is possible to predict active site residues involved in binding and catalysis. These predictions, and thus also the model, can be tested by protein engineering experiments. © 1995 Wiley‐Liss, Inc.