1w79: Difference between revisions

Revision as of 16:41, 21 February 2008

CRYSTAL STRUCTURE OF THE DD-TRANSPEPTIDASE-CARBOXYPEPTIDASE FROM ACTINOMADURA R39

OverviewOverview

Actinomadura sp. R39 produces an exocellular DD-peptidase/penicillin-binding protein (PBP) whose primary structure is similar to that of Escherichia coli PBP4. It is characterized by a high beta-lactam-binding activity (second order rate constant for the acylation of the active site serine by benzylpenicillin: k2/K = 300 mm(-1) s(-1)). The crystal structure of the DD-peptidase from Actinomadura R39 was solved at a resolution of 1.8 angstroms by single anomalous dispersion at the cobalt resonance wavelength. The structure is composed of three domains: a penicillin-binding domain similar to the penicillin-binding domain of E. coli PBP5 and two domains of unknown function. In most multimodular PBPs, additional domains are generally located at the C or N termini of the penicillin-binding domain. In R39, the other two domains are inserted in the penicillin-binding domain, between the SXXK and SXN motifs, in a manner similar to "Matryoshka dolls." One of these domains is composed of a five-stranded beta-sheet with two helices on one side, and the other domain is a double three-stranded beta-sheet inserted in the previous domain. Additionally, the 2.4-angstroms structure of the acyl-enzyme complex of R39 with nitrocefin reveals the absence of active site conformational change upon binding the beta-lactams.

About this StructureAbout this Structure

1W79 is a Single protein structure of sequence from [1] with and as ligands. Active as Serine-type D-Ala-D-Ala carboxypeptidase, with EC number 3.4.16.4 Known structural/functional Site: . Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the Actinomadura R39 DD-peptidase reveals new domains in penicillin-binding proteins., Sauvage E, Herman R, Petrella S, Duez C, Bouillenne F, Frere JM, Charlier P, J Biol Chem. 2005 Sep 2;280(35):31249-56. Epub 2005 Jun 29. PMID:15987687

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 ==Overview==
-Actinomadura sp. R39 produces an exocellular, DD-peptidase/penicillin-binding protein (PBP) whose primary structure is, similar to that of Escherichia coli PBP4. It is characterized by a high, beta-lactam-binding activity (second order rate constant for the acylation, of the active site serine by benzylpenicillin: k2/K = 300 mm(-1) s(-1))., The crystal structure of the DD-peptidase from Actinomadura R39 was solved, at a resolution of 1.8 angstroms by single anomalous dispersion at the, cobalt resonance wavelength. The structure is composed of three domains: a, penicillin-binding domain similar to the penicillin-binding domain of E., coli PBP5 and two domains of unknown function. In most multimodular PBPs, additional domains are generally located at the C or N termini of the, penicillin-binding domain. In R39, the other two domains are inserted in, the penicillin-binding domain, between the SXXK and SXN motifs, in a, manner similar to "Matryoshka dolls." One of these domains is composed of, a five-stranded beta-sheet with two helices on one side, and the other, domain is a double three-stranded beta-sheet inserted in the previous, domain. Additionally, the 2.4-angstroms structure of the acyl-enzyme, complex of R39 with nitrocefin reveals the absence of active site, conformational change upon binding the beta-lactams.
+Actinomadura sp. R39 produces an exocellular DD-peptidase/penicillin-binding protein (PBP) whose primary structure is similar to that of Escherichia coli PBP4. It is characterized by a high beta-lactam-binding activity (second order rate constant for the acylation of the active site serine by benzylpenicillin: k2/K = 300 mm(-1) s(-1)). The crystal structure of the DD-peptidase from Actinomadura R39 was solved at a resolution of 1.8 angstroms by single anomalous dispersion at the cobalt resonance wavelength. The structure is composed of three domains: a penicillin-binding domain similar to the penicillin-binding domain of E. coli PBP5 and two domains of unknown function. In most multimodular PBPs, additional domains are generally located at the C or N termini of the penicillin-binding domain. In R39, the other two domains are inserted in the penicillin-binding domain, between the SXXK and SXN motifs, in a manner similar to "Matryoshka dolls." One of these domains is composed of a five-stranded beta-sheet with two helices on one side, and the other domain is a double three-stranded beta-sheet inserted in the previous domain. Additionally, the 2.4-angstroms structure of the acyl-enzyme complex of R39 with nitrocefin reveals the absence of active site conformational change upon binding the beta-lactams.
 ==About this Structure==
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 [[Category: Charlier, P.]]
 [[Category: Duez, C.]]
-[[Category: Frere, J.M.]]
+[[Category: Frere, J M.]]
 [[Category: Herman, R.]]
 [[Category: Petrella, S.]]
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 [[Category: transpeptidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:20:11 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:41:12 2008''