Penicillin-binding protein

From Proteopedia

(Difference between revisions)

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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]]'>
 == Function ==
+'''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].
-'''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.
+'''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'''.
+See also:
+*[[DD-transpeptidase (Hebrew)]].
+*[[Sandbox 126|Penicillin-binding proteins and antibiotics]]
+For ''Mycobacterium tuberculosis'' PBP complex with penicillin see [[Mycobacterium Tuberculosis Transpeptidase Domain]].
 == Relevance ==
 PBP inhibition by antibiotics leads to irregularities in the cell wall and eventual bacterial death<ref>PMID:11369864</ref>.
+See also [[How B-lactam drugs work]].
 == Structural highlights ==
@@ Line 16: / Line 24: @@
 </StructureSection>
-==3D structures of penicillin-binding protein==
-Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-{{#tree:id=OrganizedByTopic|openlevels=0|
-*'''Penicillin-binding protein'''
-**[[1qme]], [[1rp5]], [[2z2l]], [[5oau]] – SpPBP 2X – ''Streptococcus pneumoniae''<br />
-**[[1k25]], [[1pyy]] – SpPBP 2X (mutant) <br />
-**[[5u47]] - PBP 2X – ''Streptococcus thermophilus''<br />
-**[[2fff]] - SpPBP 1B<br />
-**[[2bg1]], [[2xd5]] - SpPBP 1B (mutant) <br />
-**[[2c6w]], [[2v2f]] - SpPBP 1A <br />
-**[[2wad]], [[2wae]], [[2waf]] – SpPBP 2B<br />
-**[[3vma]] – EcPBP 1B - ''Escherichia coli''<br />
-**[[6g5r]], [[6fzk]] – EcPBP 1B UB2H domain – NMR<br />
-**[[4bjp]] – EcPBP 3 residues 67-577<br />
-**[[4bjq]] – EcPBP 3 residues 88-165<br />
-**[[2ex2]] – EcPBP 4<br />
-**[[1nzo]], [[1nzu]] – EcPBP 5<br />
-**[[1hd8]], [[1nj4]], [[1sdn]] – EcPBP 5 (mutant) <br />
-**[[3it9]] – EcPBP 6<br />
-**[[5tro]] - SaPBP 1 dimerization and transpeptidation domains – ''Staphylococcus aureus''<br />
-**[[1mwr]], [[1vqq]], [[4bl2]], [[4bl3]], [[4cpk]] - SaPBP 2A (mutant) <br />
-**[[2olu]], [[3dwk]], [[5m1a]], [[5m19]], [[5m18]] – SaPBP 2<br />
-**[[3vsk]] - SaPBP 3<br />
-**[[1tvf]] – SaPBP 4<br />
-**[[6dz8]], [[6c3k]] – SaPBP 4 (mutant)<br />
-**[[1w5d]] – BsPBP 4A – ''Bacillus subtilis''<br />
-**[[3mfd]] – BsPBP 5*<br />
-**[[2oqo]] – AaPBP 1A – ''Aquifex aeolicus''<br />
-**[[3equ]] – NgPBP 2 – ''Neisseria gonorrhoeae''<br />
-**[[3eqv]], [[5ksh]] – NgPBP 2 (mutant) <br />
-**[[6p52]], [[6p53]] – NgPBP 2 transpeptidase domain<br />
-**[[6p56]], [[4u3t]] – NgPBP 2 transpeptidase domain (mutant)<br />
-**[[5u2g]] – HiPBP 1A – ''Haemophilus influenza''<br />
-**[[3a3d]] – HiPBP 4 <br />
-**[[3a3j]] – HiPBP 5<br />
-**[[3lo7]], [[3un7]], [[5crf]] – MtPBP A – ''Mycobacterium tuberculosis''<br />
-**[[3oc2]], [[3pbn]], [[6hr4]] – PaPBP 3 – ''Pseudomonas aeruginosa''<br />
-**[[3tg9]] – PBP – ''Bacillus halodurans''<br />
-**[[3udf]] – AbPBP – ''Acinetobacter baumannii''<br />
-**[[3zg7]] – LmPBP 4 – ''Listeria monocytogenes''<br />
-**[[5dvy]], [[5e31]] – EfPBP 2 – ''Enterococcus faecium''<br />
-**[[6bsq]] - EfPBP 4<br />
-**[[6g0k]] - EfPBP 5 (mutant)<br />
-**[[5lp4]] – HpPBP 2 – ''Helicobacter pylor''i<br />
-*Penicillin-binding protein complex with antibiotics
-**[[1qmf]], [[2z2m]], [[2zc3]], [[2zc4]], [[2zc5]], [[2zc6]], [[5oj1]], [[5oj0]], [[5oiz]] – SpPBP 2X + antibiotic<br />
-**[[1mwu]], [[1mwt]], [[1mws]] - SaPBP 2A (mutant) + antibiotic<br />
-**[[2uwx]] - SaPBP 1B (mutant) + antibiotic<br />
-**[[2olv]] - SaPBP 2 + antibiotic<br />
-**[[3zfz]], [[3zg0]], [[4dki]] - SaPBP 2’ + antibiotic<br />
-**[[3vsl]] - SaPBP 3 + antibiotic<br />
-**[[5txi]], [[5ty7]], [[5tw8]] - SaPBP 4 + antibiotic<br />
-**[[3hum]], [[3hun]], [[5ty2]], [[5tx9]], [[5tw4]] - SaPBP 4 (mutant) + antibiotic<br />
-**[[2c5w]] - SpPBP 1A + antibiotic<br />
-**[[2jch]], [[2je5]], [[2xd1]] - SpPBP 1B (mutant) + antibiotic<br />
-**[[2ex6]], [[2ex8]], [[2ex9]], [[2exa]], [[2exb]] - EcPBP 4 + antibiotic<br />
-**[[3beb]], [[3bec]], [[3mzd]], [[3mze]], [[3mzf]] - EcPBP 5 + antibiotic<br />
-**[[3ita]] - EcPBP 6 + antibiotic<br />
-**[[3fwl]], [[5hld]], [[5hlb]], [[5hla]], [[5hl9]] – EcPBP 1B + antibiotic<br />
-**[[3a3e]], [[3a3f]], [[3a3i]] – HiPBP 4 + antibiotic<br />
-**[[4oon]] – PaPBP 1A + antibiotic<br />
-**[[3ocl]], [[3ocn]], [[3pbo]], [[3pbq]], [[3pbr]], [[3pbs]], [[3pbt]], [[4kqo]], [[4kqq]], [[4kqr]], [[4l0l]], [[6un1]], [[6hr6]] – PaPBP 3 + antibiotic<br />
-**[[6hr9]] – PaPBP 3 (mutant) + antibiotic<br />
-**[[3nb6]], [[3nb7]] - AaPBP 1A + antibiotic<br />
-**[[3udi]], [[3udx]], [[3ue0]], [[3ue1]] - AbPBP + antibiotic<br />
-**[[3upn]], [[3upp]], [[5cxw]] - MtPBP A + antibiotic<br />
-**[[3upo]] - MtPBP A (mutant) + antibiotic<br />
-**[[3zg8]], [[3zg9]], [[3zga]] - LmPBP 4 + antibiotic<br />
-**[[6mkh]], [[6mki]], [[6bsr]] - EfPBP 4 + antibiotic<br />
-**[[6g88]] - EfPBP 5 + antibiotic<br />
-**[[6p54]], [[6p55]] – NgPBP 2 transpeptidase domain + antibiotic<br />
-*Penicillin-binding protein complex with boronic acid derivatives
-**[[1z6f]] – EcPBP 5 + boronic acid<br />
-**[[2y2g]], [[2y2h]], [[2y2i]], [[2y2j]], [[2y2k]], [[2y2l]], [[2y2m]], [[2y2n]], [[2y2o]], [[2y2p]], [[2y2q]] - SpPBP 1B + boronic acid derivative
-*Penicillin-binding protein complex with peptidoglycan
-**[[3itb]] - EcPBP 6 + peptidoglycan peptide<br />
-**[[2j9p]] - BsPBP 4A + peptidoglycan peptide<br />
-**[[3zg5]] - SaPBP + peptidoglycan analog<br />
-*Penicillin-binding protein complex with other inhibitors
-**[[4fsf]], [[4wel]], [[4wej]] - PaPBP 3 + inhibitor<br />
-**[[4wek]] – PaPBP 3 (mutant) + inhibitor<br />
-**[[5fgz]] – EcPBP 1B + inhibitor<br />
-**[[4cjn]] – SaPBP 2A + quinazolinine derivative<br />
-**[[6g9f]], [[6g9p]], [[6g9s]] – EcPBP 2 + inhibitor<br />
-**[[5lp5]] – HpPBP 2 + MREC <br />
-*PBP D-alanyl-D-alanine carboxypeptidase or DD-transpeptidase
-**[[1skf]] – StDADC - Streptomyces<br />
-**[[1es2]], [[1es3]], [[1es4]], [[1es5]], [[1esi]], [[1j9m]] – StDADC (mutant) <br />
-**[[1w79]], [[1w8q]], [[1w8y]] – AcDADC - Actinomadura<br />
-**[[2wke]], [[4ben]] – AcDADC + antibiotic <br />
-**[[2xk1]], [[2xln]], [[2y4a]], [[2y55]], [[2y59]], [[3zvt]], [[3zvw]], [[4b4x]], [[4b4z]] – AcDADC + boronic acid derivative <br />
-**[[2vgj]], [[2vgk]], [[2xdm]] – AcDADC + peptidoglycan analog <br />
-**[[3zcz]] – AcDADC + inhibitor <br />
-**[[4rye]] – MtDADC  <br />
-**[[4ppr]] – MtDACB1 + antibiotic <br />
-**[[5fsr]] – EcDADC  <br />
-**[[5j8x]] – EcDACA + boronic acid derivative <br />
-**[[6ntz]] – EcDADC + antibiotic <br />
-**[[6osu]] – DADC – ''Francisella tularensis'' <br />
-}}
 == References ==
 <references/>
 [[Category:Topic Page]]

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E. coli PBP 4 complex with the antibiotic ampicillin and glycerol 2ex6

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1 Function
2 Relevance
3 Structural highlights
4 3D structures of penicillin-binding protein

Function

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 Penicillin-binding proteins.

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^[1]. The PBP are classified to high-molecular weight and low-molecular weight groups. PBP 3 is also named FtsI.

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 . The contains the ^[3]. Water molecules are shown as red spheres.

3D structures of penicillin-binding protein

Penicillin-binding protein 3D structures

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