5NCK

The Crystal Structure of N-acetylmannosamine kinase in Fusobacterium nucleatum

Summary for 5NCK

• Entry DOI: 10.2210/pdb5nck/pdb
• Descriptor: N-acetylmannosamine kinase (2 entities in total)
• Functional Keywords: n-acetylmannosamine kinase, zinc-binding motif, rok family, sialic acid, transferase
• Biological source: Fusobacterium nucleatum
• Total number of polymer chains: 2
• Total formula weight: 63806.15

Authors

Caing-Carlsson, R.,Sharma, A.,Friemann, R.,Ramaswamy, S. (deposition date: 2017-03-06, release date: 2017-06-28, Last modification date: 2024-05-08)

Primary citation

Caing-Carlsson, R.,Goyal, P.,Sharma, A.,Ghosh, S.,Setty, T.G.,North, R.A.,Friemann, R.,Ramaswamy, S.
Crystal structure of N-acetylmannosamine kinase from Fusobacterium nucleatum.
Acta Crystallogr F Struct Biol Commun, 73:356-362, 2017

PubMed Abstract: 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.

PubMed: 28580924
DOI: 10.1107/S2053230X17007439

Experimental method

X-RAY DIFFRACTION (2.23 Å)