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Penicillin-binding protein

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PBP inhibition by antibiotics leads to irregularities in the cell wall and eventual bacterial death<ref>PMID:11369864</ref>.
PBP inhibition by antibiotics leads to irregularities in the cell wall and eventual bacterial death<ref>PMID:11369864</ref>.
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See also [[How B-lactam drugs work]].
== Structural highlights ==
== Structural highlights ==

Revision as of 09:33, 12 January 2020

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

Drag the structure with the mouse to rotate

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

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