Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ONO

IspC Mn2+ complex

Summary for 1ONO
Entry DOI10.2210/pdb1ono/pdb
Related1ONN 1ONP
Descriptor1-deoxy-D-xylulose 5-phosphate reductoisomerase, MANGANESE (II) ION (3 entities in total)
Functional Keywordsisoprenoid biosynthesis, mevalonate-independent pathway, ispc, oxidoreductase
Biological sourceEscherichia coli
Total number of polymer chains2
Total formula weight86973.63
Authors
Steinbacher, S.,Kaiser, J.,Eisenreich, W.,Huber, R.,Bacher, A.,Rohdich, F. (deposition date: 2003-02-28, release date: 2003-03-18, Last modification date: 2023-10-25)
Primary citationSteinbacher, S.,Kaiser, J.,Eisenreich, W.,Huber, R.,Bacher, A.,Rohdich, F.
Structural basis of fosmidomycin action revealed by the complex with 2-C-methyl-D-erythritol 4-phosphate synthase (IspC). Implications for the catalytic mechanism and anti-malaria drug development.
J.BIOL.CHEM., 278:18401-18407, 2003
Cited by
PubMed Abstract: 2-C-Methyl-d-erythritol 4-phosphate synthase (IspC) is the first enzyme committed to isoprenoid biosynthesis in the methylerythritol phosphate pathway, which represents an alternative route to the classical mevalonate pathway. As it is present in many pathogens and plants, but not in man, this pathway has attracted considerable interest as a target for novel antibiotics and herbicides. Fosmidomycin represents a specific high-affinity inhibitor of IspC. Very recently, its anti-malaria activity in man has been demonstrated in clinical trials. Here, we present the crystal structure of Escherichia coli IspC in complex with manganese and fosmidomycin at 2.5 A resolution. The (N-formyl-N-hydroxy)amino group provides two oxygen ligands to manganese that is present in a distorted octahedral coordination, whereas the phosphonate group is anchored in a specific pocket by numerous hydrogen bonds. Both sites are connected by a spacer of three methylene groups. The substrate molecule, 1-d-deoxyxylulose 5-phosphate, can be superimposed onto fosmidomycin, explaining the stereochemical course of the reaction.
PubMed: 12621040
DOI: 10.1074/jbc.M300993200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

238582

数据于2025-07-09公开中

PDB statisticsPDBj update infoContact PDBjnumon