1vbf: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1vbf.gif|left|200px]] | [[Image:1vbf.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1vbf", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1vbf| PDB=1vbf | SCENE= }} | ||
}} | |||
'''Crystal structure of protein L-isoaspartate O-methyltransferase homologue from Sulfolobus tokodaii''' | '''Crystal structure of protein L-isoaspartate O-methyltransferase homologue from Sulfolobus tokodaii''' | ||
| Line 23: | Line 20: | ||
==Reference== | ==Reference== | ||
How oligomerization contributes to the thermostability of an archaeon protein. Protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii., Tanaka Y, Tsumoto K, Yasutake Y, Umetsu M, Yao M, Fukada H, Tanaka I, Kumagai I, J Biol Chem. 2004 Jul 30;279(31):32957-67. Epub 2004 May 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15169774 15169774] | How oligomerization contributes to the thermostability of an archaeon protein. Protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii., Tanaka Y, Tsumoto K, Yasutake Y, Umetsu M, Yao M, Fukada H, Tanaka I, Kumagai I, J Biol Chem. 2004 Jul 30;279(31):32957-67. Epub 2004 May 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15169774 15169774] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfolobus tokodaii]] | [[Category: Sulfolobus tokodaii]] | ||
| Line 34: | Line 30: | ||
[[Category: Yao, M.]] | [[Category: Yao, M.]] | ||
[[Category: Yasutake, Y.]] | [[Category: Yasutake, Y.]] | ||
[[Category: | [[Category: Inter-subunit disulfide bridge]] | ||
[[Category: | [[Category: Protein repair enzyme]] | ||
[[Category: | [[Category: Trimeric coiled coil assembly]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:19:56 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 12:19, 3 May 2008
Crystal structure of protein L-isoaspartate O-methyltransferase homologue from Sulfolobus tokodaii
OverviewOverview
To study how oligomerization may contribute to the thermostability of archaeon proteins, we focused on a hexameric protein, protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii (StoPIMT). The crystal structure shows that StoPIMT has a distinctive hexameric structure composed of monomers consisting of two domains: an S-adenosylmethionine-dependent methyltransferase fold domain and a C-terminal alpha-helical domain. The hexameric structure includes three interfacial contact regions: major, minor, and coiled-coil. Several C-terminal deletion mutants were constructed and characterized. The hexameric structure and thermostability were retained when the C-terminal alpha-helical domain (Tyr(206)-Thr(231)) was deleted, suggesting that oligomerization via coiled-coil association using the C-terminal alpha-helical domains did not contribute critically to hexamerization or to the increased thermostability of the protein. Deletion of three additional residues located in the major contact region, Tyr(203)-Asp(204)-Asp(205), led to a significant decrease in hexamer stability and chemico/thermostability. Although replacement of Thr(146) and Asp(204), which form two hydrogen bonds in the interface in the major contact region, with Ala did not affect hexamer formation, these mutations led to a significant decrease in thermostability, suggesting that two residues in the major contact region make significant contributions to the increase in stability of the protein via hexamerization. These results suggest that cooperative hexamerization occurs via interactions of "hot spot" residues and that a couple of interfacial hot spot residues are responsible for enhancing thermostability via oligomerization.
About this StructureAbout this Structure
1VBF is a Single protein structure of sequence from Sulfolobus tokodaii. Full crystallographic information is available from OCA.
ReferenceReference
How oligomerization contributes to the thermostability of an archaeon protein. Protein L-isoaspartyl-O-methyltransferase from Sulfolobus tokodaii., Tanaka Y, Tsumoto K, Yasutake Y, Umetsu M, Yao M, Fukada H, Tanaka I, Kumagai I, J Biol Chem. 2004 Jul 30;279(31):32957-67. Epub 2004 May 27. PMID:15169774 Page seeded by OCA on Sat May 3 12:19:56 2008