1udx: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1udx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UDX FirstGlance]. <br> | <table><tr><td colspan='2'>[[1udx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus_hb8 Thermus thermophilus hb8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UDX FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1udx RCSB], [http://www.ebi.ac.uk/pdbsum/1udx PDBsum], [http://www.topsan.org/Proteins/RSGI/1udx TOPSAN]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1udx RCSB], [http://www.ebi.ac.uk/pdbsum/1udx PDBsum], [http://www.topsan.org/Proteins/RSGI/1udx TOPSAN]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/OBG_THET8 OBG_THET8]] An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate (By similarity). It may play a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control (Potential).[HAMAP-Rule:MF_01454] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Thermus thermophilus hb8]] | [[Category: Thermus thermophilus hb8]] | ||
[[Category: Inoue, M | [[Category: Inoue, M]] | ||
[[Category: Kukimoto-Niino, M | [[Category: Kukimoto-Niino, M]] | ||
[[Category: Kuramitsu, S | [[Category: Kuramitsu, S]] | ||
[[Category: Murayama, K | [[Category: Murayama, K]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Shirouzu, M | [[Category: Shirouzu, M]] | ||
[[Category: Yokoyama, S | [[Category: Yokoyama, S]] | ||
[[Category: Gtp-binding protein]] | [[Category: Gtp-binding protein]] | ||
[[Category: Obg]] | [[Category: Obg]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Rsgi]] | [[Category: Rsgi]] | ||
[[Category: Tgs domain]] | [[Category: Tgs domain]] | ||
Revision as of 22:48, 25 December 2014
Crystal structure of the conserved protein TT1381 from Thermus thermophilus HB8Crystal structure of the conserved protein TT1381 from Thermus thermophilus HB8
Structural highlights
Function[OBG_THET8] An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate (By similarity). It may play a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control (Potential).[HAMAP-Rule:MF_01454] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedObg 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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