2XK1

Crystal structure of a complex between Actinomadura R39 DD-peptidase and a boronate inhibitor

Summary for 2XK1

• Entry DOI: 10.2210/pdb2xk1/pdb
• Related: 1W79 1W8Q 1W8Y 2VGJ 2VGK 2WKE 2XDM
• Descriptor: D-ALANYL-D-ALANINE CARBOXYPEPTIDASE, [(1S)-1-{[(2-benzylphenyl)carbonyl]amino}ethyl](trihydroxy)borate(1-), SULFATE ION, ... (5 entities in total)
• Functional Keywords: hydrolase, peptidoglycan
• Biological source: ACTINOMADURA SP
• Cellular location: Secreted: P39045
• Total number of polymer chains: 4
• Total formula weight: 193561.30

Authors

Sauvage, E.,Herman, R.,Kerff, F.,Rocaboy, M.,Charlier, P. (deposition date: 2010-07-07, release date: 2011-01-26, Last modification date: 2024-11-13)

Primary citation

Woon, E.C.Y.,Zervosen, A.,Sauvage, E.,Simmons, K.J.,Ivec, M.,Inglis, S.R.,Fishwick, C.W.G.,Gobec, S.,Charlier, P.,Luxen, A.,Schofield, C.J.
Structure Guided Development of Potent Reversibly Binding Penicillin Binding Protein Inhibitors
Acs Med.Chem.Lett., 2:219-, 2011

PubMed Abstract: Following from the evaluation of different types of electrophiles, combined modeling and crystallographic analyses are used to generate potent boronic acid based inhibitors of a penicillin binding protein. The results suggest that a structurally informed approach to penicillin binding protein inhibition will be useful for the development of both improved reversibly binding inhibitors, including boronic acids, and acylating inhibitors, such as β-lactams.

PubMed: 24900305
DOI: 10.1021/ML100260X

Experimental method

X-RAY DIFFRACTION (2.8 Å)