4C5A
The X-ray crystal structures of D-alanyl-D-alanine ligase in complex ADP and D-cycloserine phosphate
Summary for 4C5A
| Entry DOI | 10.2210/pdb4c5a/pdb |
| Related | 4C5B 4C5C |
| Descriptor | D-ALANINE--D-ALANINE LIGASE, PEPTIDE, ADENOSINE-5'-DIPHOSPHATE, ... (7 entities in total) |
| Functional Keywords | ligase, ddlb, antibiotic |
| Biological source | ESCHERICHIA COLI K-12 More |
| Total number of polymer chains | 3 |
| Total formula weight | 74122.52 |
| Authors | Batson, S.,Majce, V.,Lloyd, A.J.,Rea, D.,Fishwick, C.W.G.,Simmons, K.J.,Fulop, V.,Roper, D.I. (deposition date: 2013-09-10, release date: 2015-01-21, Last modification date: 2023-12-20) |
| Primary citation | Batson, S.,de Chiara, C.,Majce, V.,Lloyd, A.J.,Gobec, S.,Rea, D.,Fulop, V.,Thoroughgood, C.W.,Simmons, K.J.,Dowson, C.G.,Fishwick, C.W.G.,de Carvalho, L.P.S.,Roper, D.I. Inhibition of D-Ala:D-Ala ligase through a phosphorylated form of the antibiotic D-cycloserine. Nat Commun, 8:1939-1939, 2017 Cited by PubMed Abstract: D-cycloserine is an antibiotic which targets sequential bacterial cell wall peptidoglycan biosynthesis enzymes: alanine racemase and D-alanine:D-alanine ligase. By a combination of structural, chemical and mechanistic studies here we show that the inhibition of D-alanine:D-alanine ligase by the antibiotic D-cycloserine proceeds via a distinct phosphorylated form of the drug. This mechanistic insight reveals a bimodal mechanism of action for a single antibiotic on different enzyme targets and has significance for the design of future inhibitor molecules based on this chemical structure. PubMed: 29208891DOI: 10.1038/s41467-017-02118-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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