1onp
From Proteopedia
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| - | [[Image:1onp.gif|left|200px]] | + | [[Image:1onp.gif|left|200px]] |
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| - | '''IspC complex with Mn2+ and fosmidomycin''' | + | {{Structure |
| + | |PDB= 1onp |SIZE=350|CAPTION= <scene name='initialview01'>1onp</scene>, resolution 2.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=FOM:3-[FORMYL(HYDROXY)AMINO]PROPYLPHOSPHONIC ACID'>FOM</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/1-deoxy-D-xylulose-5-phosphate_reductoisomerase 1-deoxy-D-xylulose-5-phosphate reductoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.267 1.1.1.267] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''IspC complex with Mn2+ and fosmidomycin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ONP is a [ | + | 1ONP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ONP OCA]. |
==Reference== | ==Reference== | ||
| - | 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., Steinbacher S, Kaiser J, Eisenreich W, Huber R, Bacher A, Rohdich F, J Biol Chem. 2003 May 16;278(20):18401-7. Epub 2003 Mar 5. PMID:[http:// | + | 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., Steinbacher S, Kaiser J, Eisenreich W, Huber R, Bacher A, Rohdich F, J Biol Chem. 2003 May 16;278(20):18401-7. Epub 2003 Mar 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12621040 12621040] |
[[Category: 1-deoxy-D-xylulose-5-phosphate reductoisomerase]] | [[Category: 1-deoxy-D-xylulose-5-phosphate reductoisomerase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: mevalonate-independent pathway]] | [[Category: mevalonate-independent pathway]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:13:15 2008'' |
Revision as of 11:13, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | and | ||||||
| Activity: | 1-deoxy-D-xylulose-5-phosphate reductoisomerase, with EC number 1.1.1.267 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
IspC complex with Mn2+ and fosmidomycin
Overview
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.
About this Structure
1ONP is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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., Steinbacher S, Kaiser J, Eisenreich W, Huber R, Bacher A, Rohdich F, J Biol Chem. 2003 May 16;278(20):18401-7. Epub 2003 Mar 5. PMID:12621040
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