Structures of Escherichia coli tryptophanase in holo and 'semi-holo' forms

Acta Crystallographica. Section F, Structural Biology Communications
Anna KoganYehuda Goldgur

Abstract

Two crystal forms of Escherichia coli tryptophanase (tryptophan indole-lyase, Trpase) were obtained under the same crystallization conditions. Both forms belonged to the same space group P43212 but had slightly different unit-cell parameters. The holo crystal form, with pyridoxal phosphate (PLP) bound to Lys270 of both polypeptide chains in the asymmetric unit, diffracted to 2.9 Å resolution. The second crystal form diffracted to 3.2 Å resolution. Of the two subunits in the asymmetric unit, one was found in the holo form, while the other appeared to be in the apo form in a wide-open conformation with two sulfate ions bound in the vicinity of the active site. The conformation of all holo subunits is the same in both crystal forms. The structures suggest that Trpase is flexible in the apo form. Its conformation partially closes upon binding of PLP. The closed conformation might correspond to the enzyme in its active state with both cofactor and substrate bound in a similar way as in tyrosine phenol-lyase.

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Oct 27, 2004·Acta Crystallographica. Section D, Biological Crystallography·Anna KoganYehuda Goldgur
Jun 23, 2006·Acta Crystallographica. Section D, Biological Crystallography·Shao Yang KuP Lynne Howell
Aug 21, 2007·Acta Crystallographica. Section D, Biological Crystallography·Natalia TsesinOrna Almog
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Apr 5, 2011·Acta Crystallographica. Section D, Biological Crystallography·Garib N MurshudovAlexei A Vagin

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Citations

Dec 3, 2015·Acta Crystallographica. Section D, Biological Crystallography·Keren GreenOrna Almog
Mar 9, 2017·Biofouling·Cristina CattòFabio Forlani
Nov 25, 2017·Biochemistry·Lu LiuPeng R Chen

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