1MDZ

Crystal structure of ArnB aminotransferase with cycloserine and pyridoxal 5' phosphate

Summary for 1MDZ

• Entry DOI: 10.2210/pdb1mdz/pdb
• Related: 1MDO 1MDX
• Descriptor: ArnB aminotransferase, D-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-N,O-CYCLOSERYLAMIDE, PYRIDOXAL-5'-PHOSPHATE, ... (4 entities in total)
• Functional Keywords: type 1 aminotransferase fold, transferase
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 1
• Total formula weight: 43412.16

Authors

Noland, B.W.,Newman, J.M.,Hendle, J.,Badger, J.,Christopher, J.A.,Tresser, J.,Buchanan, M.D.,Wright, T.,Rutter, M.E.,Sanderson, W.E.,Muller-Dieckmann, H.-J.,Gajiwala, K.S.,Sauder, J.M.,Buchanan, S.G. (deposition date: 2002-08-07, release date: 2002-12-11, Last modification date: 2025-03-26)

Primary citation

Noland, B.W.,Newman, J.M.,Hendle, J.,Badger, J.,Christopher, J.A.,Tresser, J.,Buchanan, M.D.,Wright, T.,Rutter, M.E.,Sanderson, W.E.,Muller-Dieckmann, H.-J.,Gajiwala, K.,Buchanan, S.G.
Structural studies of Salmonella typhimurium ArnB (PmrH) aminotransferase: A 4-amino-4-deoxy-L-arabinose lipopolysaccharide modifying enzyme
Structure, 10:1569-1580, 2002

PubMed Abstract: Lipid A modification with 4-amino-4-deoxy-L-arabinose confers on certain pathogenic bacteria, such as Salmonella, resistance to cationic antimicrobial peptides, including those derived from the innate immune system. ArnB catalysis of amino group transfer from glutamic acid to the 4"-position of a UDP-linked ketopyranose molecule to form UDP-4-amino-4-deoxy-L-arabinose represents a key step in the lipid A modification pathway. Structural and functional studies of the ArnB aminotransferase were undertaken by combining X-ray crystallography with biochemical analyses. High-resolution crystal structures were solved for two native forms and one covalently inhibited form of S. typhimurium ArnB. These structures permitted identification of key residues involved in substrate binding and catalysis, including a rarely observed nonprolyl cis peptide bond in the active site.

PubMed: 12429098
DOI: 10.1016/S0969-2126(02)00879-1

Experimental method

X-RAY DIFFRACTION (2.07 Å)