Beta-lactamase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:15, 30 May 2024) (edit) (undo)
 
(62 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3bm6.png|left|200px|thumb|Crystal Structure of Beta-lactamase, [[3bm6]]]]
+
<StructureSection load='' size='350' side='right' scene='45/453531/Cv/1' caption='Class B β-lactamase Ndm-1 complex with Zn+2 (grey) (PDB code [[3spu]])'>
-
{{STRUCTURE_3bm6| PDB=3bm6 | SIZE=300| SCENE=Beta-lactamase/Beta-lactamase/1|right|CAPTION=Beta-lactamase class D complex with boronic acid derivative, [[3bm6]] }}
+
__TOC__
 +
== Function ==
-
'''Beta-lactamase''' (Blac) are enzymes which make bacteria resitant to β-lactam antibiotics by breaking their β-lactam ring. Blac are classified according to their resistance targets. Class C are cephalosporinases; Class A are broad-spectrum; Class B are metalloenzymes; Class D are cloxacilanases.
+
'''Beta-lactamase''' (Blac) are enzymes which make bacteria resistant to β-lactam antibiotics by breaking their β-lactam ring. Blac are classified according to their resistance targets.<br />
-
 
+
*'''Class A''' are broad-spectrum. See also [[TEM1 Class Antibiotic Resistance Proteins]].<br />
-
 
+
*'''Class B''' are metalloenzymes. See also [[New Delhi metallo-β-lactamase 1]].<br />
-
 
+
*'''Class C''' are cephalosporinases. See also [[Class C beta-lactamase]].<br />
-
{{TOC limit|limit=2}}
+
*'''Class D''' are cloxacilanases<br />
 +
*'''Carbapenemase''' (Car) are Blac with wide hydrolytic capacities. Car can hydrolyze penicillins, cephalosporins, monobactams and carbapenems. <br />
 +
*'''Extended-spectrum Blac''' class A (ESBL) hydrolyze penicillins but not cephalosporins.<br />
 +
*'''Serine beta-lactamase''' (ClbP) has a serine-active site.
 +
*'''AmpC beta-lactamase''' (ClbP) mediate resistance to cephalosphin, cefazolin,cefoxitin and most penicillins<ref>PMID:19136439</ref>.
 +
== Relevance ==
 +
Blac makes some bacteria resistant to antibiotics like penicillin, cephamycin and carbapenems.
 +
== Structural highlights ==
 +
The <scene name='45/453531/Cv/3'>active site of class B Blac contains 2 Zn+2 ions</scene>.<ref>PMID:21774017</ref>
 +
==See also==
 +
[[Journal:Structure:1]]
== 3D Structures of Beta-lactamase ==
== 3D Structures of Beta-lactamase ==
 +
[[Beta-lactamase 3D structures]]
-
===β-lactamase class A===
+
</StructureSection>
-
 
+
-
[[3dtm]] - EcBlac A residues 24-286 (mutant) - Escherichia coli<br />
+
-
[[3c7u]], [[3c7v]] – EcBlac A (mutant) + Protein Blip<br />
+
-
[[1axb]] - EcBlac A (mutant) + transition state analog<br />
+
-
[[1tem]] - EcBlac A (mutant) + penicillanic acid derivative<br />
+
-
[[1o7e]] – Blac – Stenotrophonas maltophilia
+
-
 
+
-
===β-lactamase class B===
+
-
 
+
-
[[3fcz]], [[3i0v]], [[3i11]], [[3i13]], [[3i14]], [[3i15]] – BcBlac B - Bacillus cereus<br />
+
-
[[3knr]], [[3kns]] - BcBlac C (mutant)
+
-
 
+
-
===β-lactamase class C===
+
-
 
+
-
[[3fkw]], [[3iwi]], [[3iwo]], [[3iwq]], [[3ixd]] – EcBlac C (mutant) <br />
+
-
[[3bm6]], [[3fkv]], [[3o86]], [[3o87]], [[3o88]] – EcBlac C + boronic acid derivative<br />
+
-
[[3ixb]], [[3ixg]] - EcBlac C (mutant) + boronic acid derivative<br />
+
-
[[3ixh]] - EcBlac C (mutant) + cefotaxime<br />
+
-
[[3gqz]], [[3gr2]], [[3grj]], [[3gsg]], [[3gtc]], [[3gv9]], [[3gvb]] - EcBlac C + inhibitor
+
-
 
+
-
===β-lactamase class D===
+
-
 
+
-
[[2rl3]], [[1k55]], [[1k57]], [[1k4e]], [[1ewz]], [[1fof]] – PaBlac D – Pseudomonas aeruginosa<br />
+
-
[[2hp5]], [[2hp6]], [[2hp9]], [[2hpb]] - PaBlac D (mutant) <br />
+
-
[[1k6r]] - PaBlac D + moxalactam<br />
+
-
[[1k6s]] - PaBlac D + phenylboronic acid<br />
+
-
[[1k54]] - PaBlac D + penicillanic acid derivative<br />
+
-
 
+
-
[[1bsg]] – Blac – Streptomyces albus
+
-
 
+
-
 
+
-
 
+
 +
== References ==
 +
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Class B β-lactamase Ndm-1 complex with Zn+2 (grey) (PDB code 3spu)

Drag the structure with the mouse to rotate

References

  1. ↑ Jacoby GA. AmpC beta-lactamases. Clin Microbiol Rev. 2009 Jan;22(1):161-82, Table of Contents. PMID:19136439 doi:10.1128/CMR.00036-08
  2. ↑ King D, Strynadka N. Crystal structure of New Delhi metallo-beta-lactamase reveals molecular basis for antibiotic resistance. Protein Sci. 2011 Sep;20(9):1484-91. doi: 10.1002/pro.697. Epub 2011 Aug, 2. PMID:21774017 doi:10.1002/pro.697

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman

Retrieved from "http://52.214.119.220/wiki/index.php/Beta-lactamase"
Personal tools