1ub3: Difference between revisions

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[[Image:1ub3.jpg|left|200px]]<br /><applet load="1ub3" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ub3.jpg|left|200px]]
caption="1ub3, resolution 1.40&Aring;" />
 
'''Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8'''<br />
{{Structure
|PDB= 1ub3 |SIZE=350|CAPTION= <scene name='initialview01'>1ub3</scene>, resolution 1.40&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=HPD:1-HYDROXY-PENTANE-3,4-DIOL-5-PHOSPHATE'>HPD</scene>
|ACTIVITY= [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]
|GENE=
}}
 
'''Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8'''
 


==Overview==
==Overview==
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==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 <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].  
1UB3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UB3 OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15388928 15388928]
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:[http://www.ncbi.nlm.nih.gov/pubmed/15388928 15388928]
[[Category: Deoxyribose-phosphate aldolase]]
[[Category: Deoxyribose-phosphate aldolase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: rsgi]]
[[Category: rsgi]]
[[Category: schiff base]]
[[Category: schiff base]]
[[Category: structural genomics]]
[[Category: structural genomic]]


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Revision as of 15:29, 20 March 2008

File:1ub3.jpg


PDB ID 1ub3

Drag the structure with the mouse to rotate
, resolution 1.40Å
Ligands:
Activity: Deoxyribose-phosphate aldolase, with EC number 4.1.2.4
Coordinates: save as pdb, mmCIF, xml



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. 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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