1UDX

Crystal structure of the conserved protein TT1381 from Thermus thermophilus HB8

Summary for 1UDX

• Entry DOI: 10.2210/pdb1udx/pdb
• Descriptor: the GTP-binding protein Obg, ACETATE ION, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• Functional Keywords: gtp-binding protein, obg, tgs domain, riken structural genomics/proteomics initiative, rsgi, structural genomics, protein binding
• Biological source: Thermus thermophilus
• Total number of polymer chains: 1
• Total formula weight: 44795.07

Authors

Kukimoto-Niino, M.,Shirouzu, M.,Murayama, K.,Inoue, M.,Kuramitsu, S.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-05-07, release date: 2004-03-16, Last modification date: 2023-12-27)

Primary citation

Kukimoto-Niino, M.,Murayama, K.,Inoue, M.,Terada, T.,Tame, J.R.,Kuramitsu, S.,Shirouzu, M.,Yokoyama, S.
Crystal structure of the GTP-binding protein Obg from Thermus thermophilus HB8.
J.Mol.Biol., 337:761-770, 2004

PubMed Abstract: 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.

PubMed: 15019792
DOI: 10.1016/j.jmb.2004.01.047

Experimental method

X-RAY DIFFRACTION (2.07 Å)