Penicillin-binding protein

From Proteopedia

spinqualitylabelsall models E. coli PBP 4 complex with the antibiotic ampicillin and glycerol 2ex6 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Structural highlights 4 3D structures of penicillin-binding protein Function Penicillin-binding protein or peptidoglycan d,d-transpeptidase (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]. See also How B-lactam drugs work. 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

References

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