1i52: Difference between revisions
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|PDB= 1i52 |SIZE=350|CAPTION= <scene name='initialview01'>1i52</scene>, resolution 1.50Å | |PDB= 1i52 |SIZE=350|CAPTION= <scene name='initialview01'>1i52</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CTP:CYTIDINE-5'-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ISPD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= ISPD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i52 OCA], [http://www.ebi.ac.uk/pdbsum/1i52 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i52 RCSB]</span> | |||
}} | }} | ||
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[[Category: Noel, J P.]] | [[Category: Noel, J P.]] | ||
[[Category: Richard, S B.]] | [[Category: Richard, S B.]] | ||
[[Category: cytidylyltransferase]] | [[Category: cytidylyltransferase]] | ||
[[Category: deoxyxylulose-5-phosphate pathway (dxp)]] | [[Category: deoxyxylulose-5-phosphate pathway (dxp)]] | ||
[[Category: isoprenoid biosynthesy]] | [[Category: isoprenoid biosynthesy]] | ||
[[Category: mep]] | [[Category: mep,]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:14:46 2008'' |
Revision as of 21:14, 30 March 2008
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, resolution 1.50Å | |||||||
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Ligands: | , , | ||||||
Gene: | ISPD (Escherichia coli) | ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
CRYSTAL STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS
OverviewOverview
The YgbP protein of Escherichia coli encodes the enzyme 4-diphosphocytidyl-2-C-methylerythritol (CDP-ME) synthetase, a member of the cytidyltransferase family of enzymes. CDP-ME is an intermediate in the mevalonate-independent pathway for isoprenoid biosynthesis in a number of prokaryotic organisms, algae, the plant plastids and the malaria parasite. Because vertebrates synthesize isoprenoid precursors using a mevalonate pathway, CDP-ME synthetase and other enzymes of the mevalonate-independent pathway for isoprenoid production represent attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs. The high-resolution structures of E. coli CDP-ME synthetase in the apo form and complexed with both CTP-Mg2+ and CDP-ME-Mg2+ reveal the stereochemical principles underlying both substrate and product recognition as well as catalysis in CDP-ME synthetase. Moreover, these complexes represent the first experimental structures for any cytidyltransferase with both substrates and products bound.
About this StructureAbout this Structure
1I52 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structure of 4-diphosphocytidyl-2-C- methylerythritol synthetase involved in mevalonate- independent isoprenoid biosynthesis., Richard SB, Bowman ME, Kwiatkowski W, Kang I, Chow C, Lillo AM, Cane DE, Noel JP, Nat Struct Biol. 2001 Jul;8(7):641-8. PMID:11427897
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