4tv5 | pdb_00004tv5

Crystal Structure of Citrate Synthase SbnG

spinqualitylabelsall models 4tv5, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4tv5 is a 1 chain structure with sequence from Staphylococcus aureus subsp. aureus str. Newman. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H3K9Z0_STAAE Publication Abstract from PubMed In response to iron deprivation, Staphylococcus aureus produces staphyloferrin B, a citrate-containing siderophore that delivers iron back to the cell. This bacterium also possesses a second citrate synthase, SbnG, that is necessary for supplying citrate to the staphyloferrin B biosynthetic pathway. We present the structure of SbnG bound to the inhibitor calcium and an active site variant in complex with oxaloacetate. The overall fold of SbnG is structurally distinct from TCA cycle citrate synthases, yet similar to metal-dependent class II aldolases. Phylogenetic analyses revealed that SbnG forms a separate clade with homologs from other siderophore biosynthetic gene clusters and is representative of a metal-independent subgroup in the phosphoenolpyruvate/pyruvate domain superfamily. A structural superposition of the SbnG active site to TCA cycle citrate synthases and site-directed mutagenesis suggests a case for convergent evolution towards a conserved catalytic mechanism for citrate production. SbnG, a Citrate Synthase in Staphylococcus aureus: a New Fold on an Old Enzyme.,Kobylarz MJ, Grigg JC, Sheldon JR, Heinrichs DE, Murphy ME J Biol Chem. 2014 Oct 21. pii: jbc.M114.603175. PMID:25336653 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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