4m54 | pdb_00004m54

The structure of the staphyloferrin B precursor biosynthetic enzyme SbnB bound to N-(1-amino-1-carboxyl-2-ethyl)-glutamic acid and NADH

spinqualitylabelsall models 4m54, resolution 2.36Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4m54 is a 1 chain structure with sequence from Staphylococcus aureus subsp. aureus MW2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AE5, CL, NAI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H3K9Y6_STAAE Publication Abstract from PubMed 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 alpha-ketoglutarate and L-Dap. Also, we describe crystal structures of SbnB in complex with NADH and ACEGA as well as with NAD(+) and alpha-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. Synthesis of L-2,3-diaminopropionic Acid, a siderophore and antibiotic precursor.,Kobylarz MJ, Grigg JC, Takayama SJ, Rai DK, Heinrichs DE, Murphy ME Chem Biol. 2014 Mar 20;21(3):379-88. doi: 10.1016/j.chembiol.2013.12.011. Epub, 2014 Jan 30. PMID:24485762 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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