1onl

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1onl, resolution 2.50Å

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

Overview

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.

About this Structure

1ONL is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structure of Thermus thermophilus HB8 H-protein of the glycine-cleavage system, resolved by a six-dimensional molecular-replacement method., Nakai T, Ishijima J, Masui R, Kuramitsu S, Kamiya N, Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1610-8. Epub 2003, Aug 19. PMID:12925792

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