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Penicillin-binding protein

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{{STRUCTURE_2ex6| PDB=2ex6 | SIZE=400| SCENE= |right|CAPTION=E. coli PBP 4 complex with antibiotic and glycerol [[2ex6]]}}
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{{STRUCTURE_2ex6| PDB=2ex6 | SIZE=400| SCENE= |right|CAPTION=E. coli PBP 4 complex with the antibiotic ampicillin and glycerol [[2ex6]]}}
== Function ==
== Function ==

Revision as of 10:12, 19 June 2016

Template:STRUCTURE 2ex6

Contents

Function

Penicillin-binding protein (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. D-alanyl-D-alanine carboxypeptidase (DDP) which cross-links peptidoglycan chains is also PBP.

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 3 domain structure. The active site contains the covalently bonded Ser62[3].

3D structures of penicillin-binding protein

Updated on 19-June-2016

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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Michal Harel, Alexander Berchansky, Joel L. Sussman

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