6mfk

Crystal Structure of Chloramphenicol Acetyltransferase from Elizabethkingia anophelis

spinqualitylabelsall models 6mfk, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6mfk is a 1 chain structure with sequence from Elizabethkingia anophelis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: MPD, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function X5KVH4_9FLAO Publication Abstract from PubMed Elizabethkingia anophelis is an emerging multidrug resistant pathogen that has caused several global outbreaks. E. anophelis belongs to the large family of Flavobacteriaceae, which contains many bacteria that are plant, bird, fish, and human pathogens. Several antibiotic resistance genes are found within the E. anophelis genome, including a chloramphenicol acetyltransferase (CAT). CATs play important roles in antibiotic resistance and can be transferred in genetic mobile elements. They catalyse the acetylation of the antibiotic chloramphenicol, thereby reducing its effectiveness as a viable drug for therapy. Here, we determined the high-resolution crystal structure of a CAT protein from the E. anophelis NUHP1 strain that caused a Singaporean outbreak. Its structure does not resemble that of the classical Type A CATs but rather exhibits significant similarity to other previously characterized Type B (CatB) proteins from Pseudomonas aeruginosa, Vibrio cholerae and Vibrio vulnificus, which adopt a hexapeptide repeat fold. Moreover, the CAT protein from E. anophelis displayed high sequence similarity to other clinically validated chloramphenicol resistance genes, indicating it may also play a role in resistance to this antibiotic. Our work expands the very limited structural and functional coverage of proteins from Flavobacteriaceae pathogens which are becoming increasingly more problematic. Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1.,Ghafoori SM, Robles AM, Arada AM, Shirmast P, Dranow DM, Mayclin SJ, Lorimer DD, Myler PJ, Edwards TE, Kuhn ML, Forwood JK Sci Rep. 2021 May 4;11(1):9453. doi: 10.1038/s41598-021-88672-z. PMID:33947893 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chloramphenicol acetyltransferase 3D structures

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