3UPB
1.5 Angstrom Resolution Crystal Structure of Transaldolase from Francisella tularensis in Covalent Complex with Arabinose-5-Phosphate
Summary for 3UPB
| Entry DOI | 10.2210/pdb3upb/pdb |
| Related | 3IGX 3TE9 3TK7 3TKF 3TNO |
| Descriptor | Transaldolase, HEXAETHYLENE GLYCOL, ARABINOSE-5-PHOSPHATE, ... (6 entities in total) |
| Functional Keywords | structural genomics, center for structural genomics of infectious diseases, csgid, alpha-beta barrel/tim barrel, transferase |
| Biological source | Francisella tularensis subsp. tularensis |
| Cellular location | Cytoplasm : Q5NFX0 |
| Total number of polymer chains | 2 |
| Total formula weight | 78211.32 |
| Authors | Light, S.H.,Minasov, G.,Shuvalova, L.,Papazisi, L.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2011-11-17, release date: 2011-11-30, Last modification date: 2024-11-06) |
| Primary citation | Light, S.H.,Anderson, W.F. Arabinose 5-phosphate covalently inhibits transaldolase. J.Struct.Funct.Genom., 15:41-44, 2014 Cited by PubMed Abstract: 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. PubMed: 24510200DOI: 10.1007/s10969-014-9174-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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