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| {{STRUCTURE_1ub3| PDB=1ub3 | SCENE= }} | | {{STRUCTURE_1ub3| PDB=1ub3 | SCENE= }} |
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| '''Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8'''
| | ===Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15388928}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15388928 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15388928}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Schiff base]] | | [[Category: Schiff base]] |
| [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:59:15 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:41:59 2008'' |
