1udx: Difference between revisions
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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... |
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[[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== | ||
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[[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.]] | ||
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[[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'' | ||