6h5e

Crystal Structure of the GatD/MurT Enzyme Complex from Staphylococcus aureus with bound AMPPNP

spinqualitylabelsall models 6h5e, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6h5e is a 4 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885 and Staan. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 144, ANP, GOL, MG, PEG, ZN Related: 6gs2 Gene: SA1707 (STAAN), BTN44_02275, C3B39_12565, EP54_01845, EQ90_00760, HMPREF3211_01062 ("Micrococcus aureus" (Rosenbach 1884) Zopf 1885) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The peptidoglycan of Staphylococcus aureus is highly amidated. Amidation of alpha-D-isoglutamic acid in position 2 of the stem peptide plays a decisive role in the polymerization of cell wall building blocks. S. aureus mutants with a reduced degree of amidation are less viable and show increased susceptibility to methicillin, indicating that targeting the amidation reaction could be a useful strategy to combat this pathogen. The enzyme complex that catalyzes the formation of alpha-D-isoglutamine in the Lipid II stem peptide was identified recently and shown to consist of two subunits, the glutamine amidotransferase-like protein GatD and the Mur ligase homolog MurT. We have solved the crystal structure of the GatD/MurT complex at high resolution, revealing an open, boomerang-shaped conformation in which GatD is docked onto one end of MurT. Putative active site residues cluster at the interface between GatD and MurT and are contributed by both proteins, thus explaining the requirement for the assembled complex to carry out the reaction. Site-directed mutagenesis experiments confirm the validity of the observed interactions. Small-angle X-ray scattering data show that the complex has a similar conformation in solution, although some movement at domain interfaces can occur, allowing the two proteins to approach each other during catalysis. Several other Gram-positive pathogens, including Streptococcus pneumoniae, Clostridium perfringens and Mycobacterium tuberculosis have homologous enzyme complexes. Combined with established biochemical assays, the structure of the GatD/MurT complex provides a solid basis for inhibitor screening in S. aureus and other pathogens. Structural basis of cell wall peptidoglycan amidation by the GatD/MurT complex of Staphylococcus aureus.,Noldeke ER, Muckenfuss LM, Niemann V, Muller A, Stork E, Zocher G, Schneider T, Stehle T Sci Rep. 2018 Aug 28;8(1):12953. doi: 10.1038/s41598-018-31098-x. PMID:30154570 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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