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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Biological process
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response to antibiotic
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2 terms
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Biochemical function
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hydrolase activity
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4 terms
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Protein Sci
9:1402-1406
(2000)
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PubMed id:
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Structural effects of the active site mutation cysteine to serine in Bacillus cereus zinc-beta-lactamase.
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L.Chantalat,
E.Duée,
M.Galleni,
J.M.Frère,
O.Dideberg.
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ABSTRACT
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Beta-lactamases are involved in bacterial resistance. Members of the
metallo-enzyme class are now found in many pathogenic bacteria and are becoming
thus of major clinical importance. Despite the availability of Zn-beta-lactamase
X-ray structures their mechanism of action is still unclear. One puzzling
observation is the presence of one or two zincs in the active site. To aid in
assessing the role of zinc content in beta-lactam hydrolysis, the replacement by
Ser of the zinc-liganding residue Cys168 in the Zn-beta-lactamase from Bacillus
cereus strain 569/H/9 was carried out: the mutant enzyme (C168S) is inactive in
the mono-Zn form, but active in the di-Zn form. The structure of the mono-Zn
form of the C168S mutant has been determined at 1.85 A resolution. Ser168
occupies the same position as Cys168 in the wild-type enzyme. The protein
residues mostly affected by the mutation are Asp90-Arg91 and His210. A critical
factor for the activity of the mono-Zn species is the distance between Asp90 and
the Zn ion, which is controlled by Arg91: a slight movement of Asp90 impairs
catalysis. The evolution of a large superfamily including Zn-beta-lactamases
suggests that they may not all share the same mechanism.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Y.Yamaguchi,
N.Takashio,
J.Wachino,
Y.Yamagata,
Y.Arakawa,
K.Matsuda,
and
H.Kurosaki
(2010).
Structure of metallo-beta-lactamase IND-7 from a Chryseobacterium indologenes clinical isolate at 1.65-A resolution.
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J Biochem, 147,
905-915.
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PDB code:
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J.Antony,
N.Gresh,
L.Olsen,
L.Hemmingsen,
C.J.Schofield,
and
R.Bauer
(2002).
Binding of D- and L-captopril inhibitors to metallo-beta-lactamase studied by polarizable molecular mechanics and quantum mechanics.
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J Comput Chem, 23,
1281-1296.
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I.C.Materon,
and
T.Palzkill
(2001).
Identification of residues critical for metallo-beta-lactamase function by codon randomization and selection.
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Protein Sci, 10,
2556-2565.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
