4MP8

Staphyloferrin B precursor biosynthetic enzyme SbnB bound to malonate and NAD+

4MP8 の概要

• エントリーDOI: 10.2210/pdb4mp8/pdb
• 関連するPDBエントリー: 4M54 4MP3 4MP6 4MPD
• 分子名称: Putative ornithine cyclodeaminase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, MALONATE ION, ... (4 entities in total)
• 機能のキーワード: siderophore, l-dap synthesis, acega dehydrogenase, oxidoreductase
• 由来する生物種: Staphylococcus aureus subsp. aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38838.42

構造登録者

Grigg, J.C.,Kobylarz, M.J.,Rai, D.K.,Murphy, M.E.P. (登録日: 2013-09-12, 公開日: 2014-03-05, 最終更新日: 2024-02-28)

主引用文献

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

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: 24485762
DOI: 10.1016/j.chembiol.2013.12.011

実験手法

X-RAY DIFFRACTION (1.85 Å)