Structure of the dihydrolipoamide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form: a tale of a common protein crystallization contaminant

Andi, Babak; Soares, Alexei S.; Shi, Wuxian; Fuchs, Martin R.; McSweeney, Sean; Liu, Qun

doi:10.1107/S2053230X19011488

Title: Structure of the dihydrolipoamide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form: a tale of a common protein crystallization contaminant

Journal Article · Thu Aug 29 00:00:00 EDT 2019 · Acta Crystallographica. Section F, Structural Biology Communications

DOI:https://doi.org/10.1107/S2053230X19011488· OSTI ID:1561244

^[1]; Soares, Alexei S. ^[1]; Shi, Wuxian ^[1];

^[1];

^[1]

Brookhaven National Lab. (BNL), Upton, NY (United States)

The crystallization of amidase, the ultimate enzyme in the Trp-dependent auxin-biosynthesis pathway, from Arabidopsis thaliana was attempted using protein samples with at least 95% purity. Cube-shaped crystals that were assumed to be amidase crystals that belonged to space groupI4 (unit-cell parameters a = b = 128.6, c= 249.7 Å) were obtained and diffracted to 3.0 Å resolution. Molecular replacement using structures from the PDB containing the amidase signature fold as search models was unsuccessful in yielding a convincing solution. Using theSequence-Independent Molecular replacement Based on Available Databases(SIMBAD) program, it was discovered that the structure corresponded to dihydrolipoamide succinyltransferase from Escherichia coli(PDB entry 1c4t), which is considered to be a common crystallization contaminant protein. The structure was refined to an R_work of 23.0% and an R_free of 27.2% at 3.0 Å resolution. The structure was compared with others of the same protein deposited in the PDB. This is the first report of the structure of dihydrolipoamide succinyltransferase isolated without an expression tag and in this novel crystal form.

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Research Organization:: Brookhaven National Lab. (BNL), Upton, NY (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: SC0012704

OSTI ID:: 1561244

Report Number(s):: BNL-212052-2019-JAAM; ACSFEN

Journal Information:: Acta Crystallographica. Section F, Structural Biology Communications, Vol. 75, Issue 9; ISSN 2053-230X

Publisher:: International Union of CrystallographyCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 3 works

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Title: Structure of the dihydrolipoamide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form: a tale of a common protein crystallization contaminant

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