1j2w
From Proteopedia
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'''Tetrameric Structure of aldolase from Thermus thermophilus HB8''' | '''Tetrameric Structure of aldolase from Thermus thermophilus HB8''' | ||
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[[Category: Shiromizu, I.]] | [[Category: Shiromizu, I.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
| - | [[Category: | + | [[Category: Carbinolamine]] |
| - | [[Category: | + | [[Category: Deoxyribose phospahte]] |
| - | [[Category: | + | [[Category: Riken structural genomics/proteomics initiative]] |
| - | [[Category: | + | [[Category: Rsgi]] |
| - | [[Category: | + | [[Category: Schiff base]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
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Revision as of 17:44, 2 May 2008
Tetrameric Structure of aldolase from Thermus thermophilus HB8
Overview
2-Deoxyribose-5-phosphate aldolase catalyzes a reversible aldol condensation of two aldehydes via formation of a covalent Schiff-base intermediate at the active lysine residue. The crystal structure of 2-deoxyribose-5-phosphate aldolase from Thermus thermophilus HB8 has been determined with and without the substrate at atomic resolution. This enzyme, which has a unique homotetramer structure, has been compared with the previously reported crystal structures of two orthologues from Escherichia coli and Aeropyrum pernix. In contrast to the similar alpha/beta-barrel fold of the monomers, substantial quaternary structural differences are observed between these three enzymes. Further comparison of the subunit-subunit interface areas of these aldolases showed a clear positive correlation between the interface area and the living temperature of the source organism. From these results, it is concluded that the oligomeric state of 2-deoxyribose-5-phosphate aldolase is important for the thermostability and not for the catalytic function.
About this Structure
1J2W is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability., Lokanath NK, Shiromizu I, Ohshima N, Nodake Y, Sugahara M, Yokoyama S, Kuramitsu S, Miyano M, Kunishima N, Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1816-23. Epub 2004, Sep 23. PMID:15388928 Page seeded by OCA on Fri May 2 20:44:15 2008
Categories: Single protein | Thermus thermophilus | Kunishima, N. | Kuramitsu, S. | Lokanath, N K. | Miyano, M. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shiromizu, I. | Yokoyama, S. | Carbinolamine | Deoxyribose phospahte | Riken structural genomics/proteomics initiative | Rsgi | Schiff base | Structural genomic
