2z2m: Difference between revisions

Revision as of 11:18, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2z2m.png

Template:STRUCTURE 2z2m

Cefditoren-Acylated Penicillin-Binding Protein 2X (PBP2X) from Streptococcus pneumoniaeCefditoren-Acylated Penicillin-Binding Protein 2X (PBP2X) from Streptococcus pneumoniae

Template:ABSTRACT PUBMED 17724158

About this StructureAbout this Structure

2Z2M is a Protein complex structure of sequences from Streptococcus pneumoniae. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of cefditoren complexed with Streptococcus pneumoniae penicillin-binding protein 2X: structural basis for its high antimicrobial activity., Yamada M, Watanabe T, Miyara T, Baba N, Saito J, Takeuchi Y, Ohsawa F, Antimicrob Agents Chemother. 2007 Nov;51(11):3902-7. Epub 2007 Aug 27. PMID:17724158

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Cefditoren-Acylated Penicillin-Binding Protein 2X (PBP2X) from Streptococcus pneumoniae'''
+===Cefditoren-Acylated Penicillin-Binding Protein 2X (PBP2X) from Streptococcus pneumoniae===
-==Overview==
+<!--
-Cefditoren is the active form of cefditoren pivoxil, an oral cephalosporin antibiotic used for the treatment of respiratory tract infections and otitis media caused by bacteria such as Streptococcus pneumoniae, Haemophilus influenzae, Streptococcus pyogenes, Klebsiella pneumoniae, and methicillin-susceptible strains of Staphylococcus aureus. Beta-lactam antibiotics, including cefditoren, target penicillin-binding proteins (PBPs), which are membrane-associated enzymes that play essential roles in the peptidoglycan biosynthetic process. To envision the binding of cefditoren to PBPs, we determined the crystal structure of a trypsin-digested form of PBP 2X from S. pneumoniae strain R6 complexed with cefditoren. There are two PBP 2X molecules (designated molecules 1 and 2) per asymmetric unit. The structure reveals that the orientation of Trp374 in each molecule changes in a different way upon the formation of the complex, but each forms a hydrophobic pocket. The methylthiazole group of the C-3 side chain of cefditoren fits into this binding pocket, which consists of residues His394, Trp374, and Thr526 in molecule 1 and residues His394, Asp375, and Thr526 in molecule 2. The formation of the complex is also accompanied by an induced-fit conformational change of the enzyme in the pocket to which the C-7 side chain of cefditoren binds. These features likely play a role in the high level of activity of cefditoren against S. pneumoniae.
+The line below this paragraph, {{ABSTRACT_PUBMED_17724158}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17724158 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_17724158}}
 ==About this Structure==
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 [[Category: Penicillin-binding]]
 [[Category: Peptidoglycan synthesis]]
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