3upb: Difference between revisions
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q5NFX0_FRATT Q5NFX0_FRATT] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[RuleBase:RU004155][SAAS:SAAS004730_004_006516] | [https://www.uniprot.org/uniprot/Q5NFX0_FRATT Q5NFX0_FRATT] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[RuleBase:RU004155][SAAS:SAAS004730_004_006516] | ||
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== Publication Abstract from PubMed == | |||
Arabinose 5-phosphate (A5P) is the aldopentose version of the ketohexose fructose 6-phosphate (F6P), having identical stereochemistry but lacking atoms corresponding to the 1-carbon and 1-hydroxyl. Despite structural similarity and conservation of the reactive portion of F6P, F6P acts as a substrate whereas A5P is reported to be an inhibitor of transaldolase. To address the lack of A5P reactivity we determined a crystal structure of the Francisella tularensis transaldolase in complex with A5P. This structure reveals that like F6P, A5P forms a covalent Schiff base with active site Lys135. Unlike F6P, A5P binding fails to displace an ordered active site water molecule. Retaining this water necessitates conformational changes at the A5P-protein linkage that possibly hinder reactivity. The findings presented here show the basis of A5P inhibition and suggest an unusual mechanism of competitive, reversible-covalent transaldolase regulation. | |||
Arabinose 5-phosphate covalently inhibits transaldolase.,Light SH, Anderson WF J Struct Funct Genomics. 2014 Mar;15(1):41-4. doi: 10.1007/s10969-014-9174-1., Epub 2014 Feb 9. PMID:24510200<ref>PMID:24510200</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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==See Also== | ==See Also== | ||
*[[Transaldolase 3D structures|Transaldolase 3D structures]] | *[[Transaldolase 3D structures|Transaldolase 3D structures]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 13:32, 6 November 2024
1.5 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis in Covalent Complex with Arabinose-5-Phosphate1.5 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis in Covalent Complex with Arabinose-5-Phosphate
Structural highlights
FunctionQ5NFX0_FRATT Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway (By similarity).[RuleBase:RU004155][SAAS:SAAS004730_004_006516] Publication Abstract from PubMedArabinose 5-phosphate (A5P) is the aldopentose version of the ketohexose fructose 6-phosphate (F6P), having identical stereochemistry but lacking atoms corresponding to the 1-carbon and 1-hydroxyl. Despite structural similarity and conservation of the reactive portion of F6P, F6P acts as a substrate whereas A5P is reported to be an inhibitor of transaldolase. To address the lack of A5P reactivity we determined a crystal structure of the Francisella tularensis transaldolase in complex with A5P. This structure reveals that like F6P, A5P forms a covalent Schiff base with active site Lys135. Unlike F6P, A5P binding fails to displace an ordered active site water molecule. Retaining this water necessitates conformational changes at the A5P-protein linkage that possibly hinder reactivity. The findings presented here show the basis of A5P inhibition and suggest an unusual mechanism of competitive, reversible-covalent transaldolase regulation. Arabinose 5-phosphate covalently inhibits transaldolase.,Light SH, Anderson WF J Struct Funct Genomics. 2014 Mar;15(1):41-4. doi: 10.1007/s10969-014-9174-1., Epub 2014 Feb 9. PMID:24510200[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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