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X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form.
Carfi, A.; Duee, E.; Paul-Soto, R. et al.
1998In Acta Crystallographica. Section D, Biological Crystallography, 54 (Pt 1), p. 45-57
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Keywords :
Amino Acid Sequence; Bacteroides fragilis/enzymology; Catalytic Domain; Crystallography; Crystallography, X-Ray; Metalloendopeptidases/chemistry; Models, Molecular; Molecular Sequence Data; Reproducibility of Results; Sequence Homology, Amino Acid; Zinc/chemistry; beta-Lactamases/chemistry
Abstract :
[en] beta-Lactamases are extracellular or periplasmic bacterial enzymes which confer resistance to beta-lactam antibiotics. On the basis of their catalytic mechanisms, they can be divided into two major groups: active-site serine enzymes (classes A, C and D) and the ZnII enzymes (class B). The first crystal structure of a class B enzyme, the metallo-beta-lactamase from Bacillus cereus, has been solved at 2.5 A resolution [Carfi, Pares, Duee, Galleni, Duez, Frere & Dideberg (1995). EMBO J. 14, 4914-4921]. Recently, the crystal structure of the metallo-beta-lactamase from Bacteroides fragilis has been determined in a tetragonal space group [Concha, Rasmussen, Bush & Herzberg (1996). Structure, 4, 823-836]. The structure of the metallo-beta-lactamase from B. fragilis in an orthorhombic crystal form at 2.0 A resolution is reported here. The final crystallographic R is 0.196 for all the 32501 observed reflections in the range 10-2.0 A. The refined model includes 458 residues, 437 water molecules, four zinc and two sodium ions. These structures are discussed with reference to Zn binding and activity. A catalytic mechanism is proposed which is coherent with metallo-beta-lactamases being active with either one Zn ion (as in Aeromonas hydrophila) or two Zn ions (as in B. fragilis) bound to the protein.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Carfi, A.
Duee, E.
Paul-Soto, R.
Galleni, Moreno ;  Université de Liège - ULiège
Frère, Jean-Marie ;  Université de Liège > Département des sciences de la vie > Centre d'ingénierie des protéines
Dideberg, O.
Language :
English
Title :
X-ray structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form.
Publication date :
1998
Journal title :
Acta Crystallographica. Section D, Biological Crystallography
ISSN :
0907-4449
eISSN :
1399-0047
Publisher :
Blackwell, Oxford, United Kingdom
Volume :
54
Issue :
Pt 1
Pages :
45-57
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 01 December 2015

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