3upb: Difference between revisions

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 == 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]
+<div style="background-color:#fffaf0;">
+== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3upb" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Transaldolase 3D structures|Transaldolase 3D structures]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>