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InterPro: IPR001018 Beta-lactamase, class B, conserved site

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Matches:

393 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
Matches in BioMart

Accession

IPR001018 Beta-lactamase_class-B_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00743	BETA_LACTAMASE_B_1	346
PROSITE pattern	PS00744	BETA_LACTAMASE_B_2	230
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001279 Beta-lactamase-like

GO Term annotation Help

Process

GO:0017001 antibiotic catabolic process

Function

GO:0008270 zinc ion binding
GO:0008800 beta-lactamase activity

InterPro annotation

Entry Details in BioMart

Abstract

Synonym(s): Penicillinase, Cephalosporinase

Beta-lactamases (EC:3.5.2.6) are enzymes which catalyse the hydrolysis of an amide bond in the beta-lactam ring of antibiotics belonging to the penicillin/cephalosporin family. The class B enzymes are zinc containing proteins whilst class A, C and D enzymes are serine hydrolases. Class B beta-lactamases have been described in several Gram-negative bacterial species; they seem to share the characteristic of being able to hydrolyse carbapenem compounds, new beta-lactam antibiotics of great therapeutic potential.

The conserved regions in the sequence of known class B beta-lactamases are centred on residues known to be involved in binding the zinc ion essential for the enzymes catalytic activity [1, 2].

Structural links Help

PDB - click here

SCOP: d.157.1.1

CATH: 3.60.15.10

Database links Help

PDBe-motif: PS00743 , PS00744

Enzyme: EC:3

PROSITE doc: PDOC00606

Blocks: IPB001018

COMe: PRX000480

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001018

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O08498 Carbapenem-hydrolyzing beta-lactamase blaB-1

O24495 Hydroxyacylglutathione hydrolase 1, mitochondrial

Q0I8S8 Hydroxyacylglutathione hydrolase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR017782	Hydroxyacylglutathione hydrolase
IPR001279	Beta-lactamase-like
IPR001018	Beta-lactamase, class B, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Osano E, Arakawa Y, Wacharotayankun R, Ohta M, Horii T, Ito H, Yoshimura F, Kato N. Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance. Antimicrob. Agents Chemother. 38 71-8 1994 [PubMed: 8141584] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=8141584&action=stream&blobtype=pdf
2.	Concha NO, Rasmussen BA, Bush K, Herzberg O. Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis. Structure 4 823-36 1996 [PubMed: 8805566] http://dx.doi.org/10.1016/S0969-2126(96)00089-5

Additional Reading Open in usermanual
	Gonzalez JM, Medrano Martin FJ, Costello AL, Tierney DL, Vila AJ. The Zn2 position in metallo-beta-lactamases is critical for activity: a study on chimeric metal sites on a conserved protein scaffold. J. Mol. Biol. 373 2007 1141-56 [PubMed: 17915249] http://dx.doi.org/10.1016/j.jmb.2007.08.031
	Llarrull LI, Fabiane SM, Kowalski JM, Bennett B, Sutton BJ, Vila AJ. Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity. J. Biol. Chem. 282 2007 18276-85 [PubMed: 17426028] http://dx.doi.org/10.1074/jbc.M700742200
	Bush K. Characterization of beta-lactamases. Antimicrob. Agents Chemother. 33 1989 259-63 [PubMed: 2658779] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=2658779
	Ambler RP. The structure of beta-lactamases. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 289 1980 321-31 [PubMed: 6109327] http://links.jstor.org/sici?sici=0080-4622%28198005%29289%3A1036%3C321%3ATSOBTT%3E2.0.CO%3B2-B&origin=EBI
	Lienard BM, Garau G, Horsfall L, Karsisiotis AI, Damblon C, Lassaux P, Papamicael C, Roberts GC, Galleni M, Dideberg O, Frere JM, Schofield CJ. Structural basis for the broad-spectrum inhibition of metallo-beta-lactamases by thiols. Org. Biomol. Chem. 6 2008 2282-94 [PubMed: 18563261] http://dx.doi.org/10.1039/b802311e
	Horsfall LE, Garau G, Lienard BM, Dideberg O, Schofield CJ, Frere JM, Galleni M. Competitive inhibitors of the CphA metallo-beta-lactamase from Aeromonas hydrophila. Antimicrob. Agents Chemother. 51 2007 2136-42 [PubMed: 17307979] http://dx.doi.org/10.1128/AAC.00866-06
	Nauton L, Kahn R, Garau G, Hernandez JF, Dideberg O. Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia. J. Mol. Biol. 375 2008 257-69 [PubMed: 17999929] http://dx.doi.org/10.1016/j.jmb.2007.10.036

InterPro 23.1