3upb: Difference between revisions
New page: '''Unreleased structure''' The entry 3upb is ON HOLD Authors: Light, S.H., Minasov, G., Shuvalova, L., Papazisi, L., Anderson, W.F., Center for Structural Genomics of Infectious Disease... |
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==1.5 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis in Covalent Complex with Arabinose-5-Phosphate== | |||
<StructureSection load='3upb' size='340' side='right'caption='[[3upb]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3upb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis_subsp._tularensis Francisella tularensis subsp. tularensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UPB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A5P:ARABINOSE-5-PHOSPHATE'>A5P</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3upb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3upb OCA], [https://pdbe.org/3upb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3upb RCSB], [https://www.ebi.ac.uk/pdbsum/3upb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3upb ProSAT]</span></td></tr> | |||
</table> | |||
== 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®/PubMed®, 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> | |||
[[Category: Francisella tularensis subsp. tularensis]] | |||
[[Category: Large Structures]] | |||
[[Category: Anderson WF]] | |||
[[Category: Light SH]] | |||
[[Category: Minasov G]] | |||
[[Category: Papazisi L]] | |||
[[Category: Shuvalova L]] | |||
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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