Structure and function of a serine carboxypeptidase adapted for degradation of the protein synthesis antibiotic microcin C7

Proceedings of the National Academy of Sciences of the United States of America

Volumn 109, Issue 12, 2012, Pages 4425-4430

  Agarwal, Vinayak ^a,b   Tikhonov, Anton ^a,c   Metlitskaya, Anastasia ^a   Severinov, Konstantin ^a,c,d   Nair, Satish K ^a,b,e  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^b UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^c INSTITUTE OF MOLECULAR GENETICS   (Russian Federation)

^d RUTGERS UNIVERSITY   (United States)

^e RUTGERS UNIVERSITY   (United States)

Author keywords

Protein engineering; Reaction mechanism; Self immunity; tRNA synthetase inhibitor

Indexed keywords

MICROCIN C7; POLYPEPTIDE ANTIBIOTIC AGENT; SERINE CARBOXYPEPTIDASE; UNCLASSIFIED DRUG;

ADENYLATION; ARTICLE; BIOACCUMULATION; BIOSYNTHESIS; CATALYSIS; CELL METABOLISM; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; ENZYME SUBSTRATE; GEL PERMEATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROGEN BOND; IN VITRO STUDY; NUCLEOPHILICITY; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN HYDROLYSIS; PROTEIN LOCALIZATION; PROTEIN METABOLISM; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN SYNTHESIS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; SUBSTITUTION REACTION; WILD TYPE;

AMIDES; AMINO ACYL-TRNA SYNTHETASES; BACTERIA; BACTERIOCINS; CARBOXYPEPTIDASES; CATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MUTATION; PROTEIN ENGINEERING; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS); EQUIDAE;

EID: 84858681416     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1114224109     Document Type: Article

References (22)

1. Ibba M, Soll D (2000) Aminoacyl-tRNA synthesis. Annu Rev Biochem 69:617-650.
2. Ling J, Reynolds N, Ibba M (2009) Aminoacyl-tRNA synthesis and translational quality control. Annu Rev Microbiol 63:61-78.
3. Tao J, Schimmel P (2000) Inhibitors of aminoacyl-tRNA synthetases as novel anti-infectives. Expert Opin Invest Drugs 9:1767-1775. (Pubitemid 30639327)
4. Ataide SF, Ibba M (2006) Small molecules: Big players in the evolution of protein synthesis. ACS Chem Biol 1:285-297.
5. Reader JS, et al. (2005) Major biocontrol of plant tumors targets tRNA synthetase. Science 309:1533. (Pubitemid 41266473)
6. Stefanska AL, et al. (2000) A potent seryl tRNA synthetase inhibitor SB-217452 isolated from a Streptomyces species. J Antibiot 53:1346-1353. (Pubitemid 32042463)
7. Kazakov T, et al. (2008) Escherichia coli peptidase A, B, or N can process translation inhibitor microcin C. J Bacteriol 190:2607-2610. (Pubitemid 351466357)
8. Tikhonov A, et al. (2010) The mechanism of microcin C resistance provided by the MccF peptidase. J Biol Chem 285:37944-37952.
9. Korza HJ, Bochtler M (2005) Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow. J Biol Chem280:40802-40812. (Pubitemid 41780572)
10. Hedstrom L (2002) Serine protease mechanism and specificity. Chem Rev 102: 4501-4524.
11. Schechter I, Berger A (1967) On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 27:157-162.
12. Boehr DD, et al. (2002) Analysis of the π-π stacking interactions between the aminoglycoside antibiotic kinase APH(3′)-Illa and its nucleotide analogs. Chem Biol 9:1209-1217. (Pubitemid 35348274)
13. Dougherty DA (1996) Cation-π interactions in chemistry and biology: A new view of benzene, Phe, Tyr, and Trp. Science 271:163-168.
14. Metlitskaya A, et al. (2009) Maturation of the translation inhibitor microcin C. J Bacteriol 191:2380-2387.
15. Baumann WK, Bizzozero SA, Dutler H (1970) Specificity of alpha-chymotrypsin. Dipeptide substrates. FEBS Lett 8:257-260.
16. Baumann WK, Bizzozero SA, Dutler H (1973) Kinetic investigation of the alpha-chymotrypsin- catalyzed hydrolysis of peptide substrates. The relationship between peptide-structure N-terminal to the cleaved bond and reactivity. Eur J Biochem 39:381-391.
17. Thompson RC, Blout ER (1973) Elastase-catalyzed amide hydrolysis of tri-and tetrapeptide amides. Biochemistry 12:66-71.
18. Sachdev GP, Fruton JS (1975) Kinetics of action of pepsin on fluorescent peptide substrates. Proc Natl Acad Sci USA 72:3424-3427.
19. Smith RM, Hansen DE (1998) The pH profile for the hydrolysis of a peptide bond. J Am Chem Soc 120:8910-8913.
20. Lad C, Williams NH, Wolfenden R (2003) The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases. Proc Natl Acad Sci USA 100:5607-5610. (Pubitemid 36576855)
21. Bachovchin WW, et al. (1981) Catalytic mechanism of serine proteases: Reexamination of the pH dependence of the histidyl 1J13C2-H coupling constant in the catalytic triad of alpha-lytic protease. Proc Natl Acad Sci USA 78:7323-7326. (Pubitemid 12186132)
22. Gamcsik MP, et al. (1993) Protonation of phosphoramide mustard and other phosphoramides. J Med Chem 36:3636-3645. (Pubitemid 24004361)