4TV6
Crystal Structure of Citrate Synthase Variant SbnG E151Q
Summary for 4TV6
| Entry DOI | 10.2210/pdb4tv6/pdb |
| Related | 4TV5 |
| Descriptor | 2-dehydro-3-deoxyglucarate aldolase, OXALOACETATE ION (3 entities in total) |
| Functional Keywords | siderophore biosynthesis, iron, citrate synthase, lyase |
| Biological source | Staphylococcus aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 28884.97 |
| Authors | Kobylarz, M.J.,Grigg, J.C.,Murphy, M.E.P. (deposition date: 2014-06-26, release date: 2014-10-29, Last modification date: 2023-12-27) |
| Primary citation | Kobylarz, M.J.,Grigg, J.C.,Sheldon, J.R.,Heinrichs, D.E.,Murphy, M.E. SbnG, a Citrate Synthase in Staphylococcus aureus: A NEW FOLD ON AN OLD ENZYME. J.Biol.Chem., 289:33797-33807, 2014 Cited by PubMed Abstract: 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 toward a conserved catalytic mechanism for citrate production. PubMed: 25336653DOI: 10.1074/jbc.M114.603175 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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