Penicillin-binding protein
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
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| + | ''E. coli'' PBP structure shows a distinct 3 domain structure. The active site contains the covalently bonded Ser62<ref>PMID:16411754</ref>. | ||
==3D structures of penicillin-binding protein== | ==3D structures of penicillin-binding protein== | ||
Revision as of 10:11, 19 June 2016
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
- ↑ 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
- ↑ 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
- ↑ 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
