H
IPR015956

Penicillin-binding protein, C-terminal domain superfamily

InterPro entry
Short namePeniciliin-bd_prot_C_sf
Overlapping entries
 

Description

This superfamily represents a structural motif found at the C-terminal of penicillin-binding proteins 4 (PBP4) and 5 (PBP5), as well as at the C-terminal of D-Ala-D-Ala carboxypeptidase A, a member of the MEROPS S11 peptidase family (PBP4 and PBP5 also belong to this peptidase family). These domains share a similar structure, consisting of a β-sandwich of six strands in two sheets
[1, 2]
.

Penicillin-binding proteins are beta-lactam antibiotic-sensitive bacterial enzymes required for the growth and maintenance of the peptidoglycan layer of the bacterial cell wall that protects the cell from osmotic stress. PBP4 functions as a transpeptidase, acting co-operatively with PBP2 in staphylococcal cell wall biosynthesis and susceptibility to antimicrobial agents
[3]
.

References

1.Crystal structure of wild-type penicillin-binding protein 5 from Escherichia coli: implications for deacylation of the acyl-enzyme complex. Nicholas RA, Krings S, Tomberg J, Nicola G, Davies C. J. Biol. Chem. 278, 52826-33, (2003). View articlePMID: 14555648

2.Crystal structure of a peptidoglycan synthesis regulatory factor (PBP3) from Streptococcus pneumoniae. Morlot C, Pernot L, Le Gouellec A, Di Guilmi AM, Vernet T, Dideberg O, Dessen A. J. Biol. Chem. 280, 15984-91, (2005). View articlePMID: 15596446

3.Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics. Kishida H, Unzai S, Roper DI, Lloyd A, Park SY, Tame JR. Biochemistry 45, 783-92, (2006). View articlePMID: 16411754

GO terms

biological process

cellular component

  • None

Cross References

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