6g58

Structure of the alanine racemase from Staphylococcus aureus in complex with a pyridoxal 5' phosphate-derivative

spinqualitylabelsall models 6g58, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6g58 is a 2 chain structure with sequence from Staphylococcus aureus subsp. aureus Mu50. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: ACT, CL, EOW, GOL, MPD, MRD, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ALR1_STAAM Catalyzes the interconversion of L-alanine and D-alanine. Publication Abstract from PubMed Pyridoxal phosphate (PLP) is an enzyme cofactor required for the chemical transformation of biological amines in many central cellular processes. PLP-dependent enzymes (PLP-DEs) are ubiquitous and evolutionarily diverse, making their classification based on sequence homology challenging. Here we present a chemical proteomic method for reporting on PLP-DEs using functionalized cofactor probes. We synthesized pyridoxal analogues modified at the 2'-position, which are taken up by cells and metabolized in situ. These pyridoxal analogues are phosphorylated to functional cofactor surrogates by cellular pyridoxal kinases and bind to PLP-DEs via an aldimine bond which can be rendered irreversible by NaBH4 reduction. Conjugation to a reporter tag enables the subsequent identification of PLP-DEs using quantitative, label-free mass spectrometry. Using these probes we accessed a significant portion of the Staphylococcus aureus PLP-DE proteome (73%) and annotate uncharacterized proteins as novel PLP-DEs. We also show that this approach can be used to study structural tolerance within PLP-DE active sites and to screen for off-targets of the PLP-DE inhibitor D-cycloserine. Mining the cellular inventory of pyridoxal phosphate-dependent enzymes with functionalized cofactor mimics.,Hoegl A, Nodwell MB, Kirsch VC, Bach NC, Pfanzelt M, Stahl M, Schneider S, Sieber SA Nat Chem. 2018 Oct 8. pii: 10.1038/s41557-018-0144-2. doi:, 10.1038/s41557-018-0144-2. PMID:30297752 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alanine racemase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA