1udx: Difference between revisions
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|PDB= 1udx |SIZE=350|CAPTION= <scene name='initialview01'>1udx</scene>, resolution 2.07Å | |PDB= 1udx |SIZE=350|CAPTION= <scene name='initialview01'>1udx</scene>, resolution 2.07Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1udx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1udx OCA], [http://www.ebi.ac.uk/pdbsum/1udx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1udx RCSB]</span> | |||
}} | }} | ||
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[[Category: Shirouzu, M.]] | [[Category: Shirouzu, M.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: gtp-binding protein]] | [[Category: gtp-binding protein]] | ||
[[Category: obg]] | [[Category: obg]] | ||
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[[Category: tgs domain]] | [[Category: tgs domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:08:57 2008'' | ||
Revision as of 00:08, 31 March 2008
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| , resolution 2.07Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of the conserved protein TT1381 from Thermus thermophilus HB8
OverviewOverview
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 StructureAbout this Structure
1UDX is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
ReferenceReference
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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