1udx: Difference between revisions
New page: left|200px<br /><applet load="1udx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1udx, resolution 2.07Å" /> '''Crystal structure of... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1udx.gif|left|200px]]<br /><applet load="1udx" size=" | [[Image:1udx.gif|left|200px]]<br /><applet load="1udx" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1udx, resolution 2.07Å" /> | caption="1udx, resolution 2.07Å" /> | ||
'''Crystal structure of the conserved protein TT1381 from Thermus thermophilus HB8'''<br /> | '''Crystal structure of the conserved protein TT1381 from Thermus thermophilus HB8'''<br /> | ||
==Overview== | ==Overview== | ||
Obg comprises a unique family of high-molecular mass GTPases conserved | 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== | ==About this Structure== | ||
1UDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with ACT and MPD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1UDX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=MPD:'>MPD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDX OCA]. | ||
==Reference== | ==Reference== | ||
| Line 17: | Line 17: | ||
[[Category: Kuramitsu, S.]] | [[Category: Kuramitsu, S.]] | ||
[[Category: Murayama, K.]] | [[Category: Murayama, K.]] | ||
[[Category: RSGI, RIKEN | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | ||
[[Category: Shirouzu, M.]] | [[Category: Shirouzu, M.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| Line 29: | Line 29: | ||
[[Category: tgs domain]] | [[Category: tgs domain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:23:25 2008'' | ||
Revision as of 16:23, 21 February 2008
|
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 with and as ligands. 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
Page seeded by OCA on Thu Feb 21 15:23:25 2008
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Single protein
- Thermus thermophilus
- Inoue, M.
- Kukimoto-Niino, M.
- Kuramitsu, S.
- Murayama, K.
- RSGI, RIKEN Structural Genomics/Proteomics Initiative.
- Shirouzu, M.
- Yokoyama, S.
- ACT
- MPD
- Gtp-binding protein
- Obg
- Riken structural genomics/proteomics initiative
- Rsgi
- Structural genomics
- Tgs domain