4MP6
Staphyloferrin B precursor biosynthetic enzyme SbnB bound to citrate and NAD+
Summary for 4MP6
| Entry DOI | 10.2210/pdb4mp6/pdb |
| Related | 4M54 4MP3 4MP8 4MPD |
| Descriptor | Putative ornithine cyclodeaminase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, CITRIC ACID, ... (4 entities in total) |
| Functional Keywords | siderophore, l-dap synthesis, acega dehydrogenase, oxidoreductase |
| Biological source | Staphylococcus aureus subsp. aureus |
| Total number of polymer chains | 1 |
| Total formula weight | 38928.49 |
| Authors | Grigg, J.C.,Kobylarz, M.J.,Rai, D.K.,Murphy, M.E.P. (deposition date: 2013-09-12, release date: 2014-03-05, Last modification date: 2024-02-28) |
| Primary citation | Kobylarz, M.J.,Grigg, J.C.,Takayama, S.J.,Rai, D.K.,Heinrichs, D.E.,Murphy, M.E. Synthesis of L-2,3-diaminopropionic Acid, a siderophore and antibiotic precursor. Chem.Biol., 21:379-388, 2014 Cited by PubMed Abstract: L-2,3-diaminopropionic acid (L-Dap) is an amino acid that is a precursor of antibiotics and staphyloferrin B a siderophore produced by Staphylococcus aureus. SbnA and SbnB are encoded by the staphyloferrin B biosynthetic gene cluster and are implicated in L-Dap biosynthesis. We demonstrate here that SbnA uses PLP and substrates O-phospho-L-serine and L-glutamate to produce a metabolite N-(1-amino-1-carboxyl-2-ethyl)-glutamic acid (ACEGA). SbnB is shown to use NAD(+) to oxidatively hydrolyze ACEGA to yield α-ketoglutarate and L-Dap. Also, we describe crystal structures of SbnB in complex with NADH and ACEGA as well as with NAD(+) and α-ketoglutarate to reveal the residues required for substrate binding, oxidation, and hydrolysis. SbnA and SbnB contribute to the iron sparing response of S. aureus that enables staphyloferrin B biosynthesis in the absence of an active tricarboxylic acid cycle. PubMed: 24485762DOI: 10.1016/j.chembiol.2013.12.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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