Penicillin-binding protein

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<StructureSection load='' size='350' side='right' scene='47/478544/Cv/1' caption='E. coli PBP 4 complex with the antibiotic ampicillin and glycerol [[2ex6]]'>
<StructureSection load='' size='350' side='right' scene='47/478544/Cv/1' caption='E. coli PBP 4 complex with the antibiotic ampicillin and glycerol [[2ex6]]'>
== Function ==
== Function ==
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'''Penicillin-binding protein''' (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics (except for tabtoxinine-β-lactam, which inhibits glutamine synthetase) bind to PBPs, which are essential for bacterial cell wall synthesis. PBPs are members of a subgroup of enzymes called transpeptidases. Specifically, PBPs are DD-transpeptidases. See also [https://en.wikipedia.org/wiki/Penicillin-binding_proteins Penicillin-binding proteins].
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'''Penicillin-binding protein''' or '''peptidoglycan d,d-transpeptidase''' (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.
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'''Penicillin-binding protein''' or '''peptidoglycan d,d-transpeptidase''' or '''D-alanyl-D-alanine carboxypeptidase''' (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. '''PBP 3''' is also named '''FtsI'''.
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See also:
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*[[DD-transpeptidase (Hebrew)]].
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*[[Sandbox 126|Penicillin-binding proteins and antibiotics]]
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For ''Mycobacterium tuberculosis'' PBP complex with penicillin see [[Mycobacterium Tuberculosis Transpeptidase Domain]].
== Relevance ==
== Relevance ==
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 ==
''E. coli'' PBP structure shows a distinct <scene name='47/478544/Cv/5'>3 domain structures</scene>. The <scene name='47/478544/Cv/6'>active site</scene> contains the <scene name='47/478544/Cv/7'>covalently bond between Ser62 and antibiotic ampicillin</scene><ref>PMID:16411754</ref>. Water molecules are shown as red spheres.
''E. coli'' PBP structure shows a distinct <scene name='47/478544/Cv/5'>3 domain structures</scene>. The <scene name='47/478544/Cv/6'>active site</scene> contains the <scene name='47/478544/Cv/7'>covalently bond between Ser62 and antibiotic ampicillin</scene><ref>PMID:16411754</ref>. Water molecules are shown as red spheres.
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</StructureSection>
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==3D structures of penicillin-binding protein==
==3D structures of penicillin-binding protein==
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[[Penicillin-binding protein 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*'''Penicillin-binding protein'''
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**[[1qme]], [[1rp5]], [[2z2l]] – SpPBP 2X – ''Streptococcus pneumoniae''<br />
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**[[1k25]], [[1pyy]] – SpPBP 2X (mutant) <br />
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**[[5u47]] - PBP 2X – ''Streptococcus thermophilus''<br />
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**[[2fff]] - SpPBP 1B<br />
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**[[2bg1]], [[2xd5]] - SpPBP 1B (mutant) <br />
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**[[2c6w]], [[2v2f]] - SpPBP 1A <br />
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**[[2wad]], [[2wae]], [[2waf]] – SpPBP 2B<br />
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**[[3vma]] – EcPBP 1B - ''Escherichia coli''<br />
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**[[4bjp]] – EcPBP 3 residues 67-577<br />
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**[[4bjq]] – EcPBP 3 residues 88-165<br />
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**[[2ex2]] – EcPBP 4<br />
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**[[1nzo]], [[1nzu]] – EcPBP 5<br />
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**[[1hd8]], [[1nj4]], [[1sdn]] – EcPBP 5 (mutant) <br />
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**[[3it9]] – EcPBP 6<br />
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**[[1mwr]], [[1vqq]], [[4bl2]], [[4bl3]], [[4cpk]] - SaPBP 2A (mutant) – ''Staphylococcus aureus''<br />
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**[[2olu]], [[3dwk]] – SaPBP 2<br />
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**[[3vsk]] - SaPBP 3<br />
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**[[1tvf]] – SaPBP 4<br />
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**[[1w5d]] – BsPBP 4A – ''Bacillus subtilis''<br />
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**[[3mfd]] – BsPBP 5*<br />
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**[[2oqo]] – AaPBP 1A – ''Aquifex aeolicus''<br />
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**[[3equ]] – NgPBP 2 – ''Neisseria gonorrhoeae''<br />
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**[[3eqv]] – NgPBP 2 (mutant) <br />
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**[[3a3d]] – HiPBP 4 – ''Haemophilus influenza''<br />
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**[[3a3j]] – HiPBP 5<br />
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**[[3lo7]], [[3un7]] – MtPBP A – ''Mycobacterium tuberculosis''<br />
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**[[3oc2]], [[3pbn]] – PaPBP 3 – ''Pseudomonas aeruginosa''<br />
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**[[3tg9]] – PBP – ''Bacillus halodurans''<br />
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**[[3udf]] – AbPBP – ''Acinetobacter baumannii''<br />
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**[[3zg7]] – LmPBP 4 – ''Listeria monocytogenes''<br />
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**[[5dvy]], [[5e31]] – PBP 2 – ''Enterococcus faecium''<br />
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*Penicillin-binding protein complex with antibiotics
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**[[1qmf]], [[2z2m]], [[2zc3]], [[2zc4]], [[2zc5]], [[2zc6]] – SpPBP 2X + antibiotic<br />
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**[[1mwu]], [[1mwt]], [[1mws]] - SaPBP 2A (mutant) + antibiotic<br />
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**[[2uwx]] - SaPBP 1B (mutant) + antibiotic<br />
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**[[2olv]] - SaPBP 2 + antibiotic<br />
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**[[3zfz]], [[3zg0]], [[4dki]] - SaPBP 2’ + antibiotic<br />
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**[[3vsl]] - SaPBP 3 + antibiotic<br />
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**[[5txi]] - SaPBP 4 + antibiotic<br />
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**[[3hum]], [[3hun]] - SaPBP 4 (mutant) + antibiotic<br />
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**[[2c5w]] - SpPBP 1A + antibiotic<br />
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**[[2jch]], [[2je5]], [[2xd1]] - SpPBP 1B (mutant) + antibiotic<br />
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**[[2ex6]], [[2ex8]], [[2ex9]], [[2exa]], [[2exb]] - EcPBP 4 + antibiotic<br />
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**[[3beb]], [[3bec]], [[3mzd]], [[3mze]], [[3mzf]] - EcPBP 5 + antibiotic<br />
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**[[3ita]] - EcPBP 6 + antibiotic<br />
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**[[3fwl]] – EcPBP 1B + antibiotic<br />
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**[[3a3e]], [[3a3f]], [[3a3i]] – HiPBP 4 + antibiotic<br />
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**[[3ocl]], [[3ocn]], [[3pbo]], [[3pbq]], [[3pbr]], [[3pbs]], [[3pbt]], [[4kqo]], [[4kqq]], [[4kqr]], [[4l0l]] – PaPBP 3 + antibiotic<br />
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**[[3nb6]], [[3nb7]] - AaPBP 1A + antibiotic<br />
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**[[3udi]], [[3udx]], [[3ue0]], [[3ue1]] - AbPBP + antibiotic<br />
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*Penicillin-binding protein complex with boronic acid derivatives
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**[[1z6f]] – EcPBP 5 + boronic acid<br />
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**[[2y2g]], [[2y2h]], [[2y2i]], [[2y2j]], [[2y2k]], [[2y2l]], [[2y2m]], [[2y2n]], [[2y2o]], [[2y2p]], [[2y2q]] - SpPBP 1B + boronic acid derivative
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*Penicillin-binding protein complex with peptidoglycan
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**[[3itb]] - EcPBP 6 + peptidoglycan peptide<br />
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**[[2j9p]] - BsPBP 4A + peptidoglycan peptide<br />
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**[[3zg5]] - SaPBP + peptidoglycan analog<br />
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*Penicillin-binding protein complex with other inhibitors
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**[[4fsf]] – PaPBP + inhibitor<br />
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**[[4cjn]] – SaPBP + quinazolinine derivative<br />
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

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