6fqb

MurT/GatD peptidoglycan amidotransferase complex from Streptococcus pneumoniae R6MurT/GatD peptidoglycan amidotransferase complex from Streptococcus pneumoniae R6

Structural highlights 6fqb is a 8 chain structure with sequence from "diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Gene: A4260_05845, ERS019420_00606, ERS020535_00125, ERS021368_00525, ERS022199_00743, ERS043879_01366 ("Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886), A4260_05840, AWW74_09320, CHL72_09035, CIT24_04835, CS877_04020, CSH34_00860, ERS003549_02292, ERS019166_00428, ERS019416_00232, ERS019420_00605, ERS019499_01955, ERS019595_01427, ERS020136_01107, ERS020137_00292, ERS020140_00887, ERS020142_00808, ERS020143_01959, ERS020147_00746, ERS020148_00821, ERS020178_04008, ERS020408_00223, ERS020474_01302, ERS020521_00204, ERS020522_00778, ERS020523_00656, ERS020524_01042, ERS020526_00540, ERS020526_04035, ERS020527_01973, ERS020528_00148, ERS020541_00600, ERS020692_00332, ERS020827_01405, ERS020831_02169, ERS021300_01369, ERS021447_05442, ERS021629_07046, ERS021762_02260, ERS021858_02776, ERS022045_06260, ERS022071_00358, ERS022199_00742, ERS022232_05365, ERS022363_01901, ERS022390_00924, ERS044004_01668, ERS068943_01580, ERS232497_02277, ERS232498_04930, ERS232508_01880, ERS409064_00176, ERS558328_00424, SAMEA1026345_00620, SAMEA2626854_01213, SAMEA2626872_01126 ("Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886) Activity: Adenosylcobyric acid synthase (glutamine-hydrolyzing), with EC number 6.3.5.10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The universality of peptidoglycan in bacteria underlies the broad spectrum of many successful antibiotics. However, in our times of widespread resistance, the diversity of peptidoglycan modifications offers a variety of new antibacterials targets. In some Gram-positive species such as Streptococcus pneumoniae, Staphylococcus aureus, or Mycobacterium tuberculosis, the second residue of the peptidoglycan precursor, D-glutamate, is amidated into iso-D-glutamine by the essential amidotransferase MurT/GatD complex. Here, we present the structure of this complex at 3.0 A resolution. MurT has central and C-terminal domains similar to Mur ligases with a cysteine-rich insertion, which probably binds zinc, contributing to the interface with GatD. The mechanism of amidation by MurT is likely similar to the condensation catalyzed by Mur ligases. GatD is a glutaminase providing ammonia that is likely channeled to the MurT active site through a cavity network. The structure and assay presented here constitute a knowledge base for future drug development studies. Structure of the essential peptidoglycan amidotransferase MurT/GatD complex from Streptococcus pneumoniae.,Morlot C, Straume D, Peters K, Hegnar OA, Simon N, Villard AM, Contreras-Martel C, Leisico F, Breukink E, Gravier-Pelletier C, Le Corre L, Vollmer W, Pietrancosta N, Havarstein LS, Zapun A Nat Commun. 2018 Aug 9;9(1):3180. doi: 10.1038/s41467-018-05602-w. PMID:30093673 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 6fqb, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image