The concerted action of a positive charge and hydrogen bonds dynamically regulates the pKa of the nucleophilic cysteine in the NrdH-redoxin family

Protein Science

Volumn 23, Issue 2, 2014, Pages 238-242

  Van Laer, Koen ^a,b   Oliveira, Margarida ^a,b   Wahni, Khadija ^a,b   Messens, Joris ^a,b  

^a VRIJE UNIVERSITEIT BRUSSEL   (Belgium)

^b Brussels Center for Redox Biology   (Belgium)

Author keywords

Cysteine reactivity; Hydrogen bond; Molecular dynamics; NrdH redoxin; Redox

Indexed keywords

ARGININE; CYSTEINE; GLUTAMINE; LYSINE; OXIDOREDUCTASE; PROTEIN NRDH; REDOXIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; RIBONUCLEOTIDE REDUCTASE; THIOREDOXIN; UNCLASSIFIED DRUG; VALINE;

AMINO TERMINAL SEQUENCE; ARTICLE; CORYNEBACTERIUM GLUTAMICUM; DNA REPAIR; DNA REPLICATION; ELECTRON; ENZYME ACTIVE SITE; HYDROGEN BOND; MOLECULAR DYNAMICS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; NUCLEOPHILICITY; PKA; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STATIC ELECTRICITY;

CYSTEINE REACTIVITY; HYDROGEN BOND; MOLECULAR DYNAMICS; NRDH-REDOXIN; PKA; REDOX;

AMINO ACID SEQUENCE; BINDING SITES; CATALYTIC DOMAIN; CYSTEINE; DNA REPAIR; DNA REPLICATION; ESCHERICHIA COLI PROTEINS; GLUTAREDOXINS; HYDROGEN BONDING; MYCOBACTERIUM TUBERCULOSIS; OXIDATION-REDUCTION; PROTEIN STRUCTURE, TERTIARY; THIOREDOXINS;

EID: 84900393353     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2397     Document Type: Article

References (16)

1. Rabinovitch I, Yanku M, Yeheskel A, Cohen G, Borovok I, Aharonowitz Y (2010) Staphylococcus aureus NrdH redoxin is a reductant of the class Ib ribonucleotide reductase. J Bacteriol 192:4963-4972
2. Stehr M, Schneider G, Aslund F, Holmgren A, Lindqvist Y (2001) Structural basis for the thioredoxinlike activity profile of the glutaredoxin-like NrdHredoxin from Escherichia coli. J Biol Chem 276:35836-35841
3. Jordan A, Aslund F, Pontis E, Reichard P, Holmgren A( 1997) Characterization of Escherichia coli NrdH. A glutaredoxin-like protein with a thioredoxin-like activity profile. J Biol Chem 272:18044-18050
4. Jensen KS, Hansen RE, Winther JR (2009) Kinetic and thermodynamic aspects of cellular thiol-disulfide redox regulation. Antioxid Redox Signal 11:1047-1058
5. Van Laer K, Dziewulska AM, Fislage M, Wahni K, Hbeddou A, Collet JF, Versees W, Mateos LM, Tamu Dufe V, Messens J (2013) NrdH-redoxin of Mycobacterium tuberculosis and Corynebacterium glutamicum dimerizes at high protein concentration and exclusively receives electrons from thioredoxin reductase. J Biol Chem 288:7942-7955
6. Stehr M, Lindqvist Y (2004) NrdH-redoxin of Corynebacterium ammoniagenes forms a domain-swapped dimer. Proteins 55:613-619
7. Phulera S, Mande SC (2013) The crystal structure of Mycobacterium tuberculosis NrdH at 0.87 A suggests a possible mode of its activity. Biochemistry 52:4056-4065
8. Roos G, Foloppe N, Messens J (2013) Understanding the pK(a) of redox cysteines: The key role of hydrogen bonding. Antioxid Redox Signal 18:94-127
9. Roos G, Loverix S, Geerlings P (2006) Origin of the pKa perturbation of N-terminal cysteine in alpha- and 3(10)-helices: A computational DFT study. J Phys Chem B 110:557-562
10. Foloppe N, Vlamis-Gardikas A, Nilsson L (2012) The - Cys-X1-X2-Cys- motif of reduced glutaredoxins adopts a consensus structure that explains the low pK(a) of its catalytic cysteine. Biochemistry 51:8189-8207
11. Van Laer K, Buts L, Foloppe N, Vertommen D, Van Belle K, Wahni K, Roos G, Nilsson L, Mateos LM, Rawat M, van Nuland NA, Messens J (2012) Mycoredoxin- 1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria. Mol Microbiol 86:787-804
12. Xia TH, Bushweller JH, Sodano P, Billeter M, Bjornberg O, Holmgren A, Wuthrich K (1992) NMR structure of oxidized Escherichia coli glutaredoxin: Comparison with reduced E. coli glutaredoxin and functionally related proteins. Protein Sci 1:310-321
13. Sun C, Berardi MJ, Bushweller JH (1998) The NMR solution structure of human glutaredoxin in the fully reduced form. J Mol Biol 280:687-701
14. Jao SC, English Ospina SM, Berdis AJ, Starke DW, Post CB, Mieyal JJ (2006) Computational and mutational analysis of human glutaredoxin (thioltransferase): Probing the molecular basis of the low pKa of cysteine 22 and its role in catalysis. Biochemistry 45: 4785-4796
15. Olsson MH (2011) Protein electrostatics and pKa blind predictions; contribution from empirical predictions of internal ionizable residues. Proteins 79:3333-3345
16. Markley JL, Bax A, Arata Y, Hilbers CW, Kaptein R, Sykes BD, Wright PE, Wuthrich K (1998) Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMβ-IUPAB Inter- Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy. J Biomol NMR 12:1-23