TY - JOUR T1 - Crystal structure of N-acetylmannosamine kinase from Fusobacterium nucleatum. JF - Acta Crystallogr F Struct Biol Commun Y1 - 2017 A1 - Caing-Carlsson, Rhawnie A1 - Goyal, Parveen A1 - Sharma, Amit A1 - Ghosh, Swagatha A1 - Setty, Thanuja Gangi A1 - North, Rachel A A1 - Friemann, Rosmarie A1 - Ramaswamy, S KW - Adenosine Triphosphate KW - Amino Acid Sequence KW - Bacterial Proteins KW - Binding Sites KW - Cloning, Molecular KW - Crystallography, X-Ray KW - Escherichia coli KW - Fusobacterium nucleatum KW - Gene Expression KW - Genetic Vectors KW - Hexosamines KW - Models, Molecular KW - Phosphotransferases (Alcohol Group Acceptor) KW - Protein Binding KW - Protein Conformation, alpha-Helical KW - Protein Conformation, beta-Strand KW - Protein Interaction Domains and Motifs KW - Protein Multimerization KW - Recombinant Proteins KW - Sequence Alignment KW - Sequence Homology, Amino Acid KW - Substrate Specificity AB -

Sialic acids comprise a varied group of nine-carbon amino sugars that are widely distributed among mammals and higher metazoans. Some human commensals and bacterial pathogens can scavenge sialic acids from their environment and degrade them for use as a carbon and nitrogen source. The enzyme N-acetylmannosamine kinase (NanK; EC 2.7.1.60) belongs to the transcriptional repressors, uncharacterized open reading frames and sugar kinases (ROK) superfamily. NanK catalyzes the second step of the sialic acid catabolic pathway, transferring a phosphate group from adenosine 5'-triphosphate to the C6 position of N-acetylmannosamine to generate N-acetylmannosamine 6-phosphate. The structure of NanK from Fusobacterium nucleatum was determined to 2.23 Å resolution by X-ray crystallography. Unlike other NanK enzymes and ROK family members, F. nucleatum NanK does not have a conserved zinc-binding site. In spite of the absence of the zinc-binding site, all of the major structural features of enzymatic activity are conserved.

VL - 73 IS - Pt 6 ER -