1udx

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spinqualitylabelsall models 1udx, resolution 2.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the conserved protein TT1381 from Thermus thermophilus HB8

Overview

Obg comprises a unique family of high-molecular mass GTPases conserved, from bacteria to eukaryotes. Bacterial Obg is essential for cellular, growth, sporulation, and differentiation. Here, we report the crystal, structure of the full-length form of Obg from Thermus thermophilus HB8 at, 2.07 A resolution, in the nucleotide-free state. It reveals a three-domain, arrangement, composed of the N-terminal domain, the guanine, nucleotide-binding domain (G domain), and the C-terminal domain. The, N-terminal and G domains have the Obg fold and the Ras-like fold, respectively. These global folds are similar to those of the recently, published structure of the C-terminal domain-truncated form of Obg from, Bacillus subtilis. On the other hand, the C-terminal domain of Obg was, found to have a novel fold (the OCT fold). A comparison of the, T.thermophilus and B.subtilis nucleotide-free Obg structures revealed, significant conformational changes in the switch-I and switch-II regions, of the G domain. Notably, the N-terminal domain is rotated drastically, by, almost 180 degrees, around the G domain axis. In the T.thermophilus Obg, crystal, the nucleotide-binding site of the G domain interacts with the, C-terminal domain of the adjacent molecule. These data suggest a possible, domain rearrangement of Obg, and a potential role of the C-terminal domain, in the regulation of the nucleotide-binding state.

About this Structure

1UDX is a Single protein structure of sequence from Thermus thermophilus with ACT and MPD as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the GTP-binding protein Obg from Thermus thermophilus HB8., Kukimoto-Niino M, Murayama K, Inoue M, Terada T, Tame JR, Kuramitsu S, Shirouzu M, Yokoyama S, J Mol Biol. 2004 Mar 26;337(3):761-70. PMID:15019792

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