1ub3: Difference between revisions

Revision as of 13:42, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1ub3.png

Template:STRUCTURE 1ub3

Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8Crystal Structure of Tetrameric Structure of Aldolase from thermus thermophilus HB8

Template:ABSTRACT PUBMED 15388928

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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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===
-==Overview==
+<!--
--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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 [[Category: Schiff base]]
 [[Category: Structural genomic]]
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