1ub3: Difference between revisions
New page: left|200px<br /><applet load="1ub3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ub3, resolution 1.40Å" /> '''Crystal Structure of... |
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[[Image:1ub3.jpg|left|200px]]<br /><applet load="1ub3" size=" | [[Image:1ub3.jpg|left|200px]]<br /><applet load="1ub3" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ub3, resolution 1.40Å" /> | caption="1ub3, resolution 1.40Å" /> | ||
'''Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8'''<br /> | '''Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8'''<br /> | ||
==Overview== | ==Overview== | ||
2-Deoxyribose-5-phosphate aldolase catalyzes a reversible aldol | 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== | ==About this Structure== | ||
1UB3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with HPD as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Deoxyribose-phosphate_aldolase Deoxyribose-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.4 4.1.2.4] Full crystallographic information is available from [http:// | 1UB3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=HPD:'>HPD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Deoxyribose-phosphate_aldolase Deoxyribose-phosphate aldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.4 4.1.2.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UB3 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Kunishima, N.]] | [[Category: Kunishima, N.]] | ||
[[Category: Kuramitsu, S.]] | [[Category: Kuramitsu, S.]] | ||
[[Category: Lokanath, N | [[Category: Lokanath, N K.]] | ||
[[Category: Miyano, M.]] | [[Category: Miyano, M.]] | ||
[[Category: RSGI, RIKEN | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: HPD]] | [[Category: HPD]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:22:29 2008'' | ||
Revision as of 16:22, 21 February 2008
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Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8
OverviewOverview
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 StructureAbout this Structure
1UB3 is a Single protein structure of sequence from Thermus thermophilus with as ligand. Active as Deoxyribose-phosphate aldolase, with EC number 4.1.2.4 Full crystallographic information is available from OCA.
ReferenceReference
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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- Deoxyribose-phosphate aldolase
- Single protein
- Thermus thermophilus
- Kunishima, N.
- Kuramitsu, S.
- Lokanath, N K.
- Miyano, M.
- RSGI, RIKEN Structural Genomics/Proteomics Initiative.
- Yokoyama, S.
- HPD
- Carbinolamine
- Deoxyribose phosphate
- Riken structural genomics/proteomics initiative
- Rsgi
- Schiff base
- Structural genomics