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]]}}
{{STRUCTURE_2ex6| PDB=2ex6 | SIZE=400| SCENE= |right|CAPTION=E. coli PBP 4 complex with antibiotic and glycerol [[2ex6]]}}
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== Function ==
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'''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<ref>PMID:1103132</ref>. 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.
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== Relevance ==
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'''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. Their inhibition by antibiotics leads to irregularities in the cell wall and eventual bacterial death. 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.
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PBP inhibition by antibiotics leads to irregularities in the cell wall and eventual bacterial death<ref>PMID:11369864</ref>.
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== Structural highlights ==
==3D structures of penicillin-binding protein==
==3D structures of penicillin-binding protein==
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**[[3zcz]] – AcDDP + inhibitor<br />
**[[3zcz]] – AcDDP + inhibitor<br />
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== References ==
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[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:53, 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

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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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