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3OI7

Structure of the structure of the H13A mutant of Ykr043C in complex with sedoheptulose-1,7-bisphosphate

Summary for 3OI7
Entry DOI10.2210/pdb3oi7/pdb
Related3F3K 3LG2 3LL4
DescriptorUncharacterized protein YKR043C, 1,7-di-O-phosphono-beta-D-altro-hept-2-ulofuranose, MAGNESIUM ION, ... (7 entities in total)
Functional Keywordsbeta-furanose, structural genomics, psi-2, protein structure initiative, midwest center for structural genomics, mcsg, alpha-beta, sedoheptulose-1, 7-bisphosphatase, phosphatase, hydrolase
Biological sourceSaccharomyces cerevisiae (yeast)
Total number of polymer chains4
Total formula weight136929.00
Authors
Primary citationClasquin, M.F.,Melamud, E.,Singer, A.,Gooding, J.R.,Xu, X.,Dong, A.,Cui, H.,Campagna, S.R.,Savchenko, A.,Yakunin, A.F.,Rabinowitz, J.D.,Caudy, A.A.
Riboneogenesis in yeast.
Cell(Cambridge,Mass.), 145:969-980, 2011
Cited by
PubMed Abstract: Glucose is catabolized in yeast via two fundamental routes, glycolysis and the oxidative pentose phosphate pathway, which produces NADPH and the essential nucleotide component ribose-5-phosphate. Here, we describe riboneogenesis, a thermodynamically driven pathway that converts glycolytic intermediates into ribose-5-phosphate without production of NADPH. Riboneogenesis begins with synthesis, by the combined action of transketolase and aldolase, of the seven-carbon bisphosphorylated sugar sedoheptulose-1,7-bisphosphate. In the pathway's committed step, sedoheptulose bisphosphate is hydrolyzed to sedoheptulose-7-phosphate by the enzyme sedoheptulose-1,7-bisphosphatase (SHB17), whose activity we identified based on metabolomic analysis of the corresponding knockout strain. The crystal structure of Shb17 in complex with sedoheptulose-1,7-bisphosphate reveals that the substrate binds in the closed furan form in the active site. Sedoheptulose-7-phosphate is ultimately converted by known enzymes of the nonoxidative pentose phosphate pathway to ribose-5-phosphate. Flux through SHB17 increases when ribose demand is high relative to demand for NADPH, including during ribosome biogenesis in metabolically synchronized yeast cells.
PubMed: 21663798
DOI: 10.1016/j.cell.2011.05.022
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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数据于2025-11-05公开中

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