1UB3

Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8

Summary for 1UB3

• Entry DOI: 10.2210/pdb1ub3/pdb
• Descriptor: Aldolase protein, 1-HYDROXY-PENTANE-3,4-DIOL-5-PHOSPHATE (3 entities in total)
• Functional Keywords: schiff base, deoxyribose phosphate, carbinolamine, structural genomics, riken structural genomics/proteomics initiative, rsgi, lyase
• Biological source: Thermus thermophilus
• Total number of polymer chains: 4
• Total formula weight: 94207.55

Authors

Lokanath, N.K.,Miyano, M.,Yokoyama, S.,Kuramitsu, S.,Kunishima, N.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-03-28, release date: 2003-04-08, Last modification date: 2024-11-06)

Primary citation

Lokanath, N.K.,Shiromizu, I.,Ohshima, N.,Nodake, Y.,Sugahara, M.,Yokoyama, S.,Kuramitsu, S.,Miyano, M.,Kunishima, N.
Structure of aldolase from Thermus thermophilus HB8 showing the contribution of oligomeric state to thermostability.
Acta Crystallogr.,Sect.D, 60:1816-1823, 2004

PubMed Abstract: 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.

PubMed: 15388928
DOI: 10.1107/S0907444904020190

Experimental method

X-RAY DIFFRACTION (1.4 Å)