6PBR

Catalytic domain of E.coli dihydrolipoamide succinyltransferase in I4 space group

6PBR の概要

• エントリーDOI: 10.2210/pdb6pbr/pdb
• 分子名称: Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, SODIUM ION (3 entities in total)
• 機能のキーワード: dihydrolipoamide succinyltransferase, 2-oxoglutarate dehydrogenase multienzyme complex, tca cycle, citric acid cycle, krebs cycle, transferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 156782.46

構造登録者

Andi, B.,Soares, A.S.,Shi, W.,Fuchs, M.R.,McSweeney, S.,Liu, Q. (登録日: 2019-06-14, 公開日: 2019-06-26, 最終更新日: 2023-10-11)

主引用文献

Andi, B.,Soares, A.S.,Shi, W.,Fuchs, M.R.,McSweeney, S.,Liu, Q.
Structure of the dihydrolipoamide succinyltransferase catalytic domain from Escherichia coli in a novel crystal form: a tale of a common protein crystallization contaminant.
Acta Crystallogr.,Sect.F, 75:616-624, 2019

PubMed Abstract: 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 group I4 (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 the Sequence-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 of 23.0% and an R 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.

PubMed: 31475929
DOI: 10.1107/S2053230X19011488

実験手法

X-RAY DIFFRACTION (3 Å)