Crystal structure of N-acetylmannosamine kinase from Fusobacterium nucleatum
(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
- Caing-Carlsson, Rhawnie ; Goyal, Parveen ; Sharma, Amit LU ; Ghosh, Swagatha ; Setty, Thanuja Gangi ; North, Rachel A. ; Friemann, Rosmarie and Ramaswamy, S.
- organization
- publishing date
- 2017-06-01
- 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
-
- pmid:28580924
- wos:000402553700008
- scopus:85020294199
- 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
- 2024-04-14 13:17:00
@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}},
keywords = {{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}},
doi = {{10.1107/S2053230X17007439}},
volume = {{73}},
year = {{2017}},
}