4BJP

Crystal structure of E. coli penicillin binding protein 3

Summary for 4BJP

• Entry DOI: 10.2210/pdb4bjp/pdb
• Related: 4BJQ
• Descriptor: PENICILLIN BINDING PROTEIN TRANSPEPTIDASE DOMAIN PROTEIN, SULFATE ION, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID, ... (7 entities in total)
• Functional Keywords: transferase
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 1
• Total formula weight: 58095.50

Authors

Sauvage, E.,Joris, M.,Herman, R.,Kerff, F.,Rocaboy, M.,Charlier, P. (deposition date: 2013-04-19, release date: 2014-05-07, Last modification date: 2023-12-20)

Primary citation

Sauvage, E.,Derouaux, A.,Fraipont, C.,Joris, M.,Herman, R.,Rocaboy, M.,Schloesser, M.,Dumas, J.,Kerff, F.,Nguyen-Disteche, M.,Charlier, P.
Crystal Structure of Penicillin-Binding Protein 3 (Pbp3) from Escherichia Coli.
Plos One, 9:98042-, 2014

PubMed Abstract: In Escherichia coli, penicillin-binding protein 3 (PBP3), also known as FtsI, is a central component of the divisome, catalyzing cross-linking of the cell wall peptidoglycan during cell division. PBP3 is mainly periplasmic, with a 23 residues cytoplasmic tail and a single transmembrane helix. We have solved the crystal structure of a soluble form of PBP3 (PBP3(57-577)) at 2.5 Å revealing the two modules of high molecular weight class B PBPs, a carboxy terminal module exhibiting transpeptidase activity and an amino terminal module of unknown function. To gain additional insight, the PBP3 Val88-Ser165 subdomain (PBP3(88-165)), for which the electron density is poorly defined in the PBP3 crystal, was produced and its structure solved by SAD phasing at 2.1 Å. The structure shows a three dimensional domain swapping with a β-strand of one molecule inserted between two strands of the paired molecule, suggesting a possible role in PBP3(57-577) dimerization.

PubMed: 24875494
DOI: 10.1371/JOURNAL.PONE.0098042

Experimental method

X-RAY DIFFRACTION (2.5 Å)