Penicillin binding protein

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Ribbon model of the PBP3 from Pseudomonas aeruginosa
Common structural element of the β-lactam antibiotics, the β-lactam

A penicillin binding protein (PBP) is a protein that can bind penicillin .

properties

Penicillin binding proteins bind to β-lactam antibiotics with medium to high affinity , with the exception of tabtoxinin β-lactam . Penicillin-binding proteins have a PASTA - protein domain ( english PBP and serine / threonine kinase Associated domain , ') for binding of β-lactam antibiotics. The PASTA domain is typical of penicillin-binding proteins and protein kinase B-type proteins, which is where the acronym for the name of the domain comes from. Penicillin-binding proteins are mostly proteins of the last steps in the biosynthesis of peptidoglycan in the bacterial cell wall , e.g. As the murein -Transpeptidase.

Examples

In Escherichia coli at least six PBP come between 40 kDa before and 91 kDa. These include a D-alanine carboxypeptidase , a peptidoglycan transpeptidase and a peptidoglycan endopeptidase. A PBP of 49.5 kDa has been described in Mycobacterium smegmatis . The PBP penicillin binding protein 2A ( PBP2A ) is involved in the antibiotic resistance of MRSA .

In mitochondria of mammals , the protein exists LACTB , a homolog of the PBP βL .

Individual evidence

  1. ↑ Sainsbury, S., Bird, L., Rao, V., Shepherd, SM, Stuart, DI, Hunter, WN, Owens, RJ, and Ren, J .: Crystal Structures of Penicillin-Binding Protein 3 from Pseudomonas aeruginosa: Comparison of Native and Antibiotic-Bound Forms . In: J. Mol. Biol. . 405, 2011, pp. 173-184. doi : 10.1016 / j.jmb.2010.10.024 .
  2. ↑ JM Frère, MG Page: Penicillin-binding proteins: evergreen drug targets. In: Current Opinion in Pharmacology . Volume 18C, October 2014, pp. 112-119, doi : 10.1016 / j.coph.2014.09.012 , PMID 25450065 .
  3. ↑ a b C. Yeats, RD Finn, A. Bateman: The PASTA domain: a beta-lactam-binding domain. In: Trends in Biochemical Sciences . Volume 27, Number 9, September 2002, p. 438, PMID 12217513 .
  4. ↑ E. Sauvage, F. Kerff, M. Terrak, JA Ayala, P. Charlier: The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis. In: FEMS microbiology reviews. Volume 32, Number 2, March 2008, pp. 234-258, doi : 10.1111 / j.1574-6976.2008.00105.x , PMID 18266856 .
  5. ↑ A. Zapun, C. Contreras-Martel, T. Vernet: Penicillin-binding proteins and beta-lactam resistance. In: FEMS microbiology reviews. Volume 32, Number 2, March 2008, pp. 361-385, doi : 10.1111 / j.1574-6976.2007.00095.x , PMID 18248419 .
  6. ^ BG Spratt: Properties of the penicillin-binding proteins of Escherichia coli K12 ,. In: European Journal of Biochemistry . Volume 72, Number 2, January 1977, pp. 341-352, PMID 319999 .
  7. ↑ J. Basu, R. Chattopadhyay, M. Kundu, P. Chakrabarti: Purification and partial characterization of a penicillin-binding protein from Mycobacterium smegmatis. In: Journal of bacteriology. Volume 174, Number 14, July 1992, pp. 4829-4832, PMID 1624470 , PMC 206282 (free full text).
  8. ↑ HF Chambers: Penicillin-binding protein-mediated resistance in pneumococci and staphylococci. In: The Journal of Infectious Diseases . Volume 179 Suppl 2, March 1999, pp. S353-S359, doi : 10.1086 / 513854 , PMID 10081507 .
  9. ↑ N. Peitsaro, Z. Polianskyte, J. Tuimala, I. Pörn-Ares, J. Liobikas, O. Speer, D. Lindholm, J. Thompson, O. Eriksson: Evolution of a family of metazoan active-site serine enzymes from penicillin-binding proteins: a novel facet of the bacterial legacy. In: BMC Evolutionary Biology. Volume 8, 2008, p. 26, doi : 10.1186 / 1471-2148-8-26 , PMID 18226203 , PMC 2266909 (free full text).