Structural and functional characterization of CMP-N-acetylneuraminate synthetase from Vibrio cholerae.
Amino Acid Sequence
Bacterial Proteins
/ chemistry
Binding Sites
Catalytic Domain
Crystallization
Crystallography, X-Ray
/ methods
Cytidine Diphosphate
/ chemistry
Cytidine Monophosphate N-Acetylneuraminic Acid
/ chemistry
Cytidine Triphosphate
/ chemistry
N-Acylneuraminate Cytidylyltransferase
/ chemistry
Protein Interaction Domains and Motifs
Protein Structure, Quaternary
Sialic Acids
/ metabolism
Vibrio cholerae
/ enzymology
CMP-N-acetylneuraminate synthetase
Vibrio cholerae
function
sialic acid
structure
Journal
Acta crystallographica. Section D, Structural biology
ISSN: 2059-7983
Titre abrégé: Acta Crystallogr D Struct Biol
Pays: United States
ID NLM: 101676043
Informations de publication
Date de publication:
01 Jun 2019
01 Jun 2019
Historique:
received:
23
12
2018
accepted:
13
05
2019
entrez:
18
6
2019
pubmed:
18
6
2019
medline:
2
10
2019
Statut:
ppublish
Résumé
Several pathogenic bacteria utilize sialic acid, including host-derived N-acetylneuraminic acid (Neu5Ac), in at least two ways: they use it as a nutrient source and as a host-evasion strategy by coating themselves with Neu5Ac. Given the significant role of sialic acid in pathogenesis and host-gut colonization by various pathogenic bacteria, including Neisseria meningitidis, Haemophilus influenzae, Pasteurella multocida and Vibrio cholerae, several enzymes of the sialic acid catabolic, biosynthetic and incorporation pathways are considered to be potential drug targets. In this work, findings on the structural and functional characterization of CMP-N-acetylneuraminate synthetase (CMAS), a key enzyme in the incorporation pathway, from Vibrio cholerae are reported. CMAS catalyzes the synthesis of CMP-sialic acid by utilizing CTP and sialic acid. Crystal structures of the apo and the CDP-bound forms of the enzyme were determined, which allowed the identification of the metal cofactor Mg
Identifiants
pubmed: 31205019
pii: S2059798319006831
doi: 10.1107/S2059798319006831
pmc: PMC6580227
doi:
Substances chimiques
Bacterial Proteins
0
Sialic Acids
0
Cytidine Monophosphate N-Acetylneuraminic Acid
3063-71-6
Cytidine Diphosphate
63-38-7
Cytidine Triphosphate
65-47-4
N-Acylneuraminate Cytidylyltransferase
EC 2.7.7.43
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
564-577Subventions
Organisme : Department of Biotechnology, Ministry of Science and Technology
ID : BT/IN/SWEDEN/06/SR/2017-2018
Organisme : Department of Biotechnology, Ministry of Science and Technology
ID : BT/PR5081/INF/156/2012
Organisme : Tata Institute of Fundamental Research
ID : BT/PR12422/MED/31/287/214
Informations de copyright
open access.
Références
Biochemistry. 1999 May 11;38(19):6195-203
pubmed: 10320348
Biochem J. 1999 Oct 15;343 Pt 2:397-402
pubmed: 10510306
Glycobiology. 1999 Oct;9(10):961-78
pubmed: 10521532
J Mol Biol. 2000 Sep 8;302(1):205-17
pubmed: 10964570
J Biol Chem. 2001 Mar 16;276(11):8190-6
pubmed: 11113120
Biochem J. 2001 Sep 15;358(Pt 3):585-98
pubmed: 11577688
Glycoconj J. 2001 Mar;18(3):205-13
pubmed: 11602804
Microbiology. 2002 Nov;148(Pt 11):3681-93
pubmed: 12427958
J Mol Biol. 2003 Dec 5;334(4):625-37
pubmed: 14636592
Proc Natl Acad Sci U S A. 1992 Jun 1;89(11):4884-7
pubmed: 1534409
Infect Immun. 1992 Mar;60(3):989-97
pubmed: 1541573
Bioorg Med Chem. 2004 Dec 15;12(24):6427-35
pubmed: 15556760
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
pubmed: 15572765
Biotechnol Lett. 2006 Jan;28(2):107-13
pubmed: 16369694
Nucleic Acids Res. 2006 Jul 1;34(Web Server issue):W604-8
pubmed: 16845081
Appl Microbiol Biotechnol. 2007 Sep;76(4):827-34
pubmed: 17602221
Microbiology. 2007 Sep;153(Pt 9):2817-22
pubmed: 17768226
Trends Mol Med. 2008 Aug;14(8):351-60
pubmed: 18606570
J Inorg Biochem. 2008 Sep;102(9):1765-76
pubmed: 18614239
Infect Immun. 2008 Oct;76(10):4431-8
pubmed: 18644887
Appl Microbiol Biotechnol. 2008 Oct;80(5):757-65
pubmed: 18716769
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
pubmed: 19461840
Infect Immun. 2009 Sep;77(9):3807-16
pubmed: 19564383
J Biol Chem. 2009 Dec 18;284(51):35514-23
pubmed: 19815542
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21
pubmed: 20124702
FEBS J. 2010 Jul;277(13):2779-90
pubmed: 20491913
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42
pubmed: 21460441
Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):293-302
pubmed: 21460447
Appl Environ Microbiol. 2011 Aug 15;77(16):5782-93
pubmed: 21724895
PLoS One. 2011;6(8):e23231
pubmed: 21826242
Appl Microbiol Biotechnol. 2012 Mar;93(6):2411-23
pubmed: 21968653
Acta Crystallogr D Biol Crystallogr. 2012 Apr;68(Pt 4):368-80
pubmed: 22505257
Appl Microbiol Biotechnol. 2012 May;94(4):887-905
pubmed: 22526796
Acta Crystallogr D Biol Crystallogr. 2013 Jul;69(Pt 7):1204-14
pubmed: 23793146
Top Curr Chem. 2015;366:139-67
pubmed: 24141690
Acta Crystallogr D Biol Crystallogr. 2014 Jul;70(Pt 7):1801-11
pubmed: 25004958
Methods. 2015 Apr;76:137-148
pubmed: 25477226
Infect Immun. 2015 Aug;83(8):3126-36
pubmed: 26015477
Curr Drug Discov Technol. 2015;12(3):170-8
pubmed: 26302746
MBio. 2016 Apr 12;7(2):e02237-15
pubmed: 27073099
Biochem J. 2016 Jul 1;473(13):1905-16
pubmed: 27114558
J Med Chem. 2016 Dec 8;59(23):10343-10382
pubmed: 27607900
J Biol Chem. 1987 Dec 25;262(36):17556-62
pubmed: 2826425
Microb Biotechnol. 2018 Mar;11(2):420-428
pubmed: 29345069
FEBS Lett. 1996 Aug 5;391(1-2):157-61
pubmed: 8706906
Proteins. 1998 Feb 1;30(2):144-54
pubmed: 9489922