6MFK

Crystal Structure of Chloramphenicol Acetyltransferase from Elizabethkingia anophelis

Summary for 6MFK

• Entry DOI: 10.2210/pdb6mfk/pdb
• Descriptor: Chloramphenicol acetyltransferase, (4S)-2-METHYL-2,4-PENTANEDIOL, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: ssgcid, transferase, antibiotic resistance, structural genomics, seattle structural genomics center for infectious disease
• Biological source: Elizabethkingia anophelis
• Total number of polymer chains: 1
• Total formula weight: 24973.94

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2018-09-11, release date: 2018-10-03, Last modification date: 2023-10-11)

Primary citation

Ghafoori, S.M.,Robles, A.M.,Arada, A.M.,Shirmast, P.,Dranow, D.M.,Mayclin, S.J.,Lorimer, D.D.,Myler, P.J.,Edwards, T.E.,Kuhn, M.L.,Forwood, J.K.
Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1.
Sci Rep, 11:9453-9453, 2021

PubMed Abstract: 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.

PubMed: 33947893
DOI: 10.1038/s41598-021-88672-z

Experimental method

X-RAY DIFFRACTION (1.65 Å)