Penicillin-binding protein

Function

Penicillin-binding protein (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics (except for tabtoxinine-β-lactam, which inhibits glutamine synthetase) bind to PBPs, which are essential for bacterial cell wall synthesis. PBPs are members of a subgroup of enzymes called transpeptidases. Specifically, PBPs are DD-transpeptidases. See also Penicillin-binding proteins.

Penicillin-binding protein or peptidoglycan d,d-transpeptidase or D-alanyl-D-alanine carboxypeptidase (PBP) is a bacterial protein which binds antibiotics. There are several PBPs in each organism. PBPs are involved in the synthesis of bacterial cell wall^[1]. The PBP are classified to high-molecular weight and low-molecular weight groups. PBP 3 is also named FtsI.

Relevance

PBP inhibition by antibiotics leads to irregularities in the cell wall and eventual bacterial death^[2].

Structural highlights

E. coli PBP structure shows a distinct . The contains the ^[3]. Water molecules are shown as red spheres.

3D structures of penicillin-binding protein

Penicillin-binding protein 3D structures

E. coli PBP 4 complex with the antibiotic ampicillin and glycerol 2ex6

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Spratt BG. Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2999-3003. PMID:1103132
↑ Beadle BM, Nicholas RA, Shoichet BK. Interaction energies between beta-lactam antibiotics and E. coli penicillin-binding protein 5 by reversible thermal denaturation. Protein Sci. 2001 Jun;10(6):1254-9. PMID:11369864 doi:http://dx.doi.org/10.1110/ps.52001
↑ Kishida H, Unzai S, Roper DI, Lloyd A, Park SY, Tame JR. Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics. Biochemistry. 2006 Jan 24;45(3):783-92. PMID:16411754 doi:10.1021/bi051533t

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Alexander Berchansky, Michal Harel, Joel L. Sussman

[1] Spratt BG. Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2999-3003. PMID:1103132

[2] Beadle BM, Nicholas RA, Shoichet BK. Interaction energies between beta-lactam antibiotics and E. coli penicillin-binding protein 5 by reversible thermal denaturation. Protein Sci. 2001 Jun;10(6):1254-9. PMID:11369864 doi:http://dx.doi.org/10.1110/ps.52001

[3] Kishida H, Unzai S, Roper DI, Lloyd A, Park SY, Tame JR. Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics. Biochemistry. 2006 Jan 24;45(3):783-92. PMID:16411754 doi:10.1021/bi051533t

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