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Lokanath, N.K. et al.

Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability.

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.[1]

References

Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability. Lokanath, N.K., Shiromizu, I., Ohshima, N., Nodake, Y., Sugahara, M., Yokoyama, S., Kuramitsu, S., Miyano, M., Kunishima, N. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]

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