1ONL

Crystal structure of Thermus thermophilus HB8 H-protein of the glycine cleavage system

1ONL の概要

• エントリーDOI: 10.2210/pdb1onl/pdb
• 分子名称: glycine cleavage system H protein (2 entities in total)
• 機能のキーワード: hybrid barrel-sandwich structure, structural genomics, riken structural genomics/proteomics initiative, rsgi, oxidoreductase
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 42281.02

構造登録者

Nakai, T.,Ishijima, J.,Masui, R.,Kuramitsu, S.,Kamiya, N.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-02-28, 公開日: 2003-08-26, 最終更新日: 2023-10-25)

主引用文献

Nakai, T.,Ishijima, J.,Masui, R.,Kuramitsu, S.,Kamiya, N.
Structure of Thermus thermophilus HB8 H-protein of the glycine-cleavage system, resolved by a six-dimensional molecular-replacement method.
Acta Crystallogr.,Sect.D, 59:1610-1618, 2003

PubMed Abstract: The glycine-cleavage system is a multi-enzyme complex consisting of four different components (the P-, H-, T- and L-proteins). Recombinant H-protein corresponding to that from Thermus thermophilus HB8 has been overexpressed, purified and crystallized. Synchrotron radiation from BL44B2 at SPring-8 was used to collect a native data set to 2.5 A resolution. The crystals belonged to the hexagonal space group P6(5) and contained three molecules per asymmetric unit, with a solvent content of 39%. Because of the large number of molecules within a closely packed unit cell, this structure was solved by six-dimensional molecular replacement with the program EPMR using the pea H-protein structure as a search model and was refined to an R factor of 0.189 and a free R factor of 0.256. Comparison with the pea H-protein reveals two highly conserved regions surrounding the lipoyl-lysine arm. Both of these regions are negatively charged and each has additional properties that are conserved in H-proteins from many species, suggesting that these regions are involved in intermolecular interactions. One region has previously been proposed to constitute an interaction surface with T-protein, while the other may be involved in an interaction with P-protein. Meanwhile, the lipoyl-lysine arm of the T. thermophilus H-protein was found to be more flexible than that of the pea H-protein, supporting the hypothesis that H-protein does not form a stable complex with L-protein during the reaction.

PubMed: 12925792
DOI: 10.1107/S0907444903014975

実験手法

X-RAY DIFFRACTION (2.5 Å)