From Proteopedia
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| - | [[Image:1vbf.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1vbf| PDB=1vbf | SCENE= }} | | {{STRUCTURE_1vbf| PDB=1vbf | SCENE= }} |
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| - | '''Crystal structure of protein L-isoaspartate O-methyltransferase homologue from Sulfolobus tokodaii'''
| + | ===Crystal structure of protein L-isoaspartate O-methyltransferase homologue from Sulfolobus tokodaii=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15169774}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15169774 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15169774}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Protein repair enzyme]] | | [[Category: Protein repair enzyme]] |
| | [[Category: Trimeric coiled coil assembly]] | | [[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 Sun Jul 27 16:56:49 2008'' |
Revision as of 13:56, 27 July 2008
Template:STRUCTURE 1vbf
Crystal structure of protein L-isoaspartate O-methyltransferase homologue from Sulfolobus tokodaii
Template:ABSTRACT PUBMED 15169774
About this Structure
1VBF is a Single protein structure of sequence from Sulfolobus tokodaii. Full crystallographic information is available from OCA.
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:15169774
Page seeded by OCA on Sun Jul 27 16:56:49 2008
