d-Alanine-d-alanine ligase as a model for the activation of ATP-grasp enzymes by monovalent cations.

ATP-grasp X-ray crystallography d-alanine–d-alanine ligase (Ddl) enzyme catalysis enzyme kinetics enzyme mechanism enzyme structure metal activation metal ion–protein interaction monovalent cation structural biology

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
05 06 2020
Historique:
received: 05 02 2020
revised: 23 04 2020
pubmed: 27 4 2020
medline: 29 12 2020
entrez: 27 4 2020
Statut: ppublish

Résumé

The ATP-grasp superfamily of enzymes shares an atypical nucleotide-binding site known as the ATP-grasp fold. These enzymes are involved in many biological pathways in all domains of life. One ATP-grasp enzyme, d-alanine-d-alanine ligase (Ddl), catalyzes ATP-dependent formation of the d-alanyl-d-alanine dipeptide essential for bacterial cell wall biosynthesis and is therefore an important antibiotic drug target. Ddl is activated by the monovalent cation (MVC) K

Identifiants

pubmed: 32335509
pii: S0021-9258(17)49431-2
doi: 10.1074/jbc.RA120.012936
pmc: PMC7278361
doi:

Substances chimiques

Cations, Monovalent 0
Metals, Alkali 0
Adenosine Triphosphate 8L70Q75FXE
Peptide Synthases EC 6.3.2.-
D-alanylalanine synthetase EC 6.3.2.4

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

7894-7904

Informations de copyright

© 2020 Pederick et al.

Déclaration de conflit d'intérêts

Conflict of interest—The authors declare that they have no conflicts of interest with the contents of this article.

Références

Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42
pubmed: 21460441
Mol Syst Biol. 2011 Oct 11;7:539
pubmed: 21988835
Biochim Biophys Acta. 1990 Jan 29;1033(1):23-30
pubmed: 2302411
Proc Natl Acad Sci U S A. 2006 Oct 10;103(41):15178-83
pubmed: 17015835
J Biol Chem. 1971 Jun 10;246(11):3569-78
pubmed: 5578910
Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):8-24
pubmed: 10089390
J Biol Chem. 1962 Oct;237:3128-35
pubmed: 13938148
FEBS J. 2013 Feb;280(4):1150-66
pubmed: 23286234
Science. 1998 Apr 3;280(5360):69-77
pubmed: 9525859
J Biol Chem. 1965 Sep;240(9):3485-92
pubmed: 5891073
J Biol Chem. 2011 Jul 8;286(27):24417-25
pubmed: 21592965
J Biol Chem. 2016 Sep 30;291(40):20840-20848
pubmed: 27462078
Biochem Biophys Res Commun. 1962 Aug 7;8:377-82
pubmed: 14479178
J Biosci Bioeng. 2008 Sep;106(3):313-5
pubmed: 18930013
J Biosci Bioeng. 2005 Jun;99(6):623-8
pubmed: 16233841
Chem Biol. 2000 Jul;7(7):505-14
pubmed: 10903933
Acta Crystallogr B Struct Sci Cryst Eng Mater. 2016 Aug 1;72(Pt 4):602-25
pubmed: 27484381
J Biosci Bioeng. 2016 Aug;122(2):155-9
pubmed: 27017332
Biochemistry. 1995 Mar 7;34(9):2768-76
pubmed: 7893688
Nat Commun. 2017 Dec 5;8(1):1939
pubmed: 29208891
J Synchrotron Radiat. 2002 Nov 1;9(Pt 6):401-6
pubmed: 12409628
Methods Mol Biol. 2016;1377:111-20
pubmed: 26695027
J Biol Chem. 2006 Jan 20;281(3):1305-8
pubmed: 16267046
J Am Chem Soc. 2017 Aug 30;139(34):11803-11813
pubmed: 28768413
Exp Eye Res. 1977 Feb;24(2):145-58
pubmed: 14840
Biosci Biotechnol Biochem. 2006 Nov;70(11):2790-2
pubmed: 17090922
Biochim Biophys Acta. 1968 Apr 24;159(1):167-75
pubmed: 5650430
Proteins. 2006 Sep 1;64(4):1078-82
pubmed: 16779845
Protein Sci. 2018 Jan;27(1):112-128
pubmed: 28836357
Science. 1994 Oct 21;266(5184):439-43
pubmed: 7939684
J Biol Chem. 1972 Jul 10;247(13):4107-13
pubmed: 4556303
Open Enzym Inhib J. 2010;3:8-26
pubmed: 22180764
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32
pubmed: 15572765
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21
pubmed: 20124702
Acta Crystallogr D Biol Crystallogr. 2009 Oct;65(Pt 10):1098-106
pubmed: 19770507
Mol Cell Biochem. 1978 Feb 24;19(1):17-21
pubmed: 25379
Biochem Biophys Res Commun. 1976 Jan 12;68(1):205-10
pubmed: 2168
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):125-32
pubmed: 20124692
Biopolymers. 1983 Dec;22(12):2577-637
pubmed: 6667333
Methods Enzymol. 1985;113:393-9
pubmed: 3911005
J Bacteriol. 2005 Aug;187(15):5195-202
pubmed: 16030213
Biochem J. 1974 May;139(2):297-310
pubmed: 4447611
J Biol Chem. 1990 Jun 5;265(16):8993-8
pubmed: 2188969
Chem Rev. 1998 May 7;98(3):1067-1088
pubmed: 11848925
J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674
pubmed: 19461840
Proc Natl Acad Sci U S A. 2009 Feb 10;106(6):1737-42
pubmed: 19164768
ACS Med Chem Lett. 2013 Dec 12;4(12):1233-1237
pubmed: 24478820
Biochim Biophys Acta. 1967 Jul 11;139(2):487-501
pubmed: 6034687
J Biol Chem. 1955 Apr;213(2):813-24
pubmed: 14367342
Bioorg Med Chem. 2009 May 1;17(9):3317-23
pubmed: 19362848
J Biol Chem. 1962 Mar;237:778-86
pubmed: 14479179
Biochemistry. 1991 Feb 12;30(6):1673-82
pubmed: 1993184
Biochemistry. 1971 Mar 2;10(5):721-9
pubmed: 5544662
Acta Crystallogr B Struct Sci Cryst Eng Mater. 2016 Aug 1;72(Pt 4):626-33
pubmed: 27484382
J Med Chem. 2009 Jun 25;52(12):3814-28
pubmed: 19459643
Biosci Biotechnol Biochem. 2009 Apr 23;73(4):901-7
pubmed: 19352016

Auteurs

Jordan L Pederick (JL)

Institute for Photonics and Advanced Sensing, School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, Australia.
Department of Molecular and Cellular Biology, School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, Australia.

Andrew P Thompson (AP)

Department of Molecular and Cellular Biology, School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, Australia.

Stephen G Bell (SG)

Department of Chemistry, The University of Adelaide, Adelaide, South Australia, Australia.

John B Bruning (JB)

Institute for Photonics and Advanced Sensing, School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, Australia john.bruning@adelaide.edu.au.
Department of Molecular and Cellular Biology, School of Biological Sciences, The University of Adelaide, Adelaide, South Australia, Australia.

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