5dmx

Crystal structure of D-alanine-D-alanine ligase from Acinetobacter baumannii, space group p212121

spinqualitylabelsall models 5dmx, resolution 2.81Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dmx is a 6 chain structure with sequence from Acinetobacter baumannii ACICU. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.81Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DDL_ACIBC Cell wall formation.[HAMAP-Rule:MF_00047] Publication Abstract from PubMed Acinetobacter baumannii, which is emerging as a multidrug-resistant nosocomial pathogen, causes a number of diseases, including pneumonia, bacteremia, meningitis, and skin infections. With ATP hydrolysis, the D-alanine-D-alanine ligase (DDL) catalyzes the synthesis of D-alanyl-D-alanine, which is an essential component of bacterial peptidoglycan. In this study, we determined the crystal structure of DDL from A. baumannii (AbDDL) at a resolution of 2.2 A. The asymmetric unit contained six protomers of AbDDL. Five protomers had a closed conformation in the central domain, while one protomer had an open conformation in the central domain. The central domain with an open conformation did not interact with crystallographic symmetry-related protomers and the conformational change of the central domain was not due to crystal packing. The central domain of AbDDL can have an ensemble of the open and closed conformations before the binding of substrate ATP. The conformational change of the central domain is important for the catalytic activity and the detail information will be useful for the development of inhibitors against AbDDL and putative antibacterial agents against A. baumannii. The AbDDL structure was compared with that of other DDLs that were in complex with potent inhibitors and the catalytic activity of AbDDL was confirmed using enzyme kinetics assays. The crystal structure of the D-alanine-D-alanine ligase from Acinetobacter baumannii suggests a flexible conformational change in the central domain before nucleotide binding.,Huynh KH, Hong MK, Lee C, Tran HT, Lee SH, Ahn YJ, Cha SS, Kang LW J Microbiol. 2015 Nov;53(11):776-82. doi: 10.1007/s12275-015-5475-8. Epub 2015, Oct 28. PMID:26502962 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also D-alanine-D-alanine ligase 3D structures

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