1i52

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[[Image:1i52.gif|left|200px]]
[[Image:1i52.gif|left|200px]]
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{{Structure
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|PDB= 1i52 |SIZE=350|CAPTION= <scene name='initialview01'>1i52</scene>, resolution 1.50&Aring;
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The line below this paragraph, containing "STRUCTURE_1i52", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CTP:CYTIDINE-5&#39;-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
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|GENE= ISPD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1i52| PDB=1i52 | SCENE= }}
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|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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'''CRYSTAL STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS'''
'''CRYSTAL STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS'''
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[[Category: Noel, J P.]]
[[Category: Noel, J P.]]
[[Category: Richard, S B.]]
[[Category: Richard, S B.]]
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[[Category: cytidylyltransferase]]
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[[Category: Cytidylyltransferase]]
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[[Category: deoxyxylulose-5-phosphate pathway (dxp)]]
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[[Category: Isoprenoid biosynthesy]]
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[[Category: isoprenoid biosynthesy]]
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[[Category: Mep]]
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[[Category: mep,]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:34:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:14:46 2008''
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Revision as of 16:34, 2 May 2008

Template:STRUCTURE 1i52

CRYSTAL STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS


Overview

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 Structure

1I52 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 19:34:57 2008

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