TitleCrystal structure of N-acetylmannosamine kinase from Fusobacterium nucleatum.
Publication TypeJournal Article
Year of Publication2017
AuthorsCaing-Carlsson R, Goyal P, Sharma A, Ghosh S, Setty TGangi, North RA, Friemann R, Ramaswamy S
JournalActa Crystallogr F Struct Biol Commun
IssuePt 6
Date Published2017 Jun 01
KeywordsAdenosine Triphosphate, Amino Acid Sequence, Bacterial Proteins, Binding Sites, Cloning, Molecular, Crystallography, X-Ray, Escherichia coli, Fusobacterium nucleatum, Gene Expression, Genetic Vectors, Hexosamines, Models, Molecular, Phosphotransferases (Alcohol Group Acceptor), Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Protein Multimerization, Recombinant Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Substrate Specificity

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 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.

Alternate JournalActa Crystallogr F Struct Biol Commun
PubMed ID28580924
PubMed Central IDPMC5458393
Grant List608743 / / European Union Seventh Framework Programme / United States
2011-1759 / / The Swedish Research Council Formas / United States
2011-5790 / / The Swedish Research Council / United States
2013-04655 / / VINNOVA / United States
11:147 / / Carl Tryggers Stiftelse för Vetenskaplig Forskning / United States
1163-2014 / / European Molecular Biology Organization / United States
584-2014 / / European Molecular Biology Organization / United States
BT/IN/Sweden/41/SR/2013 / / Indo-Swedish Collaborative Grant from DBT / United States
BT/PR5081/INF/22/156/2012 / / Infrastructure Grant for the X-ray Facility from DBT / United States