7TIN
The Structure of S. aureus MenD
Summary for 7TIN
Entry DOI | 10.2210/pdb7tin/pdb |
Descriptor | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase, THIAMINE DIPHOSPHATE, GLYCINE, ... (7 entities in total) |
Functional Keywords | menaquinone biosynthesis, mend, sephchc synthase, transferase |
Biological source | Staphylococcus aureus |
Total number of polymer chains | 4 |
Total formula weight | 255674.59 |
Authors | Johnston, J.M.,Stanborough, T.,Ho, N.A.T.,Akazong, E.W.,Jiao, W. (deposition date: 2022-01-14, release date: 2022-09-14, Last modification date: 2023-10-25) |
Primary citation | Stanborough, T.,Ho, N.A.T.,Bulloch, E.M.M.,Bashiri, G.,Dawes, S.S.,Akazong, E.W.,Titterington, J.,Allison, T.M.,Jiao, W.,Johnston, J.M. Allosteric inhibition of Staphylococcus aureus MenD by 1,4-dihydroxy naphthoic acid: a feedback inhibition mechanism of the menaquinone biosynthesis pathway. Philos.Trans.R.Soc.Lond.B Biol.Sci., 378:20220035-20220035, 2023 Cited by PubMed: 36633276DOI: 10.1098/rstb.2022.0035 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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