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Crystal structure of N-acetylmannosamine kinase from Fusobacterium nucleatum

Caing-Carlsson, Rhawnie; Goyal, Parveen; Sharma, Amit LU ; Ghosh, Swagatha; Setty, Thanuja Gangi; North, Rachel A.; Friemann, Rosmarie and Ramaswamy, S. (2017) In Acta Crystallographica Section F:Structural Biology Communications 73(6). p.356-362
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... (More)

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.

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author
organization
publishing date
type
Contribution to journal
publication status
published
keywords
Fusobacterium nucleatum, N-acetylmannosamine kinase, sialic acid catabolism
in
Acta Crystallographica Section F:Structural Biology Communications
volume
73
issue
6
pages
7 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:85020294199
  • wos:000402553700008
ISSN
2053-230X
DOI
10.1107/S2053230X17007439
language
English
LU publication?
yes
id
8ab8cebc-3f74-4690-96db-69881bf1f326
date added to LUP
2017-06-28 08:34:34
date last changed
2018-01-07 12:09:27
@article{8ab8cebc-3f74-4690-96db-69881bf1f326,
  abstract     = {<p>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.</p>},
  author       = {Caing-Carlsson, Rhawnie and Goyal, Parveen and Sharma, Amit and Ghosh, Swagatha and Setty, Thanuja Gangi and North, Rachel A. and Friemann, Rosmarie and Ramaswamy, S.},
  issn         = {2053-230X},
  keyword      = {Fusobacterium nucleatum,N-acetylmannosamine kinase,sialic acid catabolism},
  language     = {eng},
  month        = {06},
  number       = {6},
  pages        = {356--362},
  publisher    = {Wiley-Blackwell},
  series       = {Acta Crystallographica Section F:Structural Biology Communications},
  title        = {Crystal structure of N-acetylmannosamine kinase from Fusobacterium nucleatum},
  url          = {http://dx.doi.org/10.1107/S2053230X17007439},
  volume       = {73},
  year         = {2017},
}