1i52
From Proteopedia
(Difference between revisions)
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<StructureSection load='1i52' size='340' side='right'caption='[[1i52]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='1i52' size='340' side='right'caption='[[1i52]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1i52]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1i52]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I52 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1i52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i52 OCA], [https://pdbe.org/1i52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i52 RCSB], [https://www.ebi.ac.uk/pdbsum/1i52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i52 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/ISPD_ECOLI ISPD_ECOLI] Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP).[HAMAP-Rule:MF_00108] |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1i52 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1i52 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | 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. | ||
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- | 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<ref>PMID:11427897</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1i52" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[MEP cytidylyltransferase|MEP cytidylyltransferase]] | *[[MEP cytidylyltransferase|MEP cytidylyltransferase]] | ||
*[[MEP cytidylyltransferase 3D structures|MEP cytidylyltransferase 3D structures]] | *[[MEP cytidylyltransferase 3D structures|MEP cytidylyltransferase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Escherichia coli K-12]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Bowman | + | [[Category: Bowman ME]] |
- | [[Category: Cane | + | [[Category: Cane DE]] |
- | [[Category: Chow | + | [[Category: Chow C]] |
- | [[Category: Kang | + | [[Category: Kang I]] |
- | [[Category: Kwiatkowski | + | [[Category: Kwiatkowski W]] |
- | [[Category: Lillo | + | [[Category: Lillo M]] |
- | [[Category: Noel | + | [[Category: Noel JP]] |
- | [[Category: Richard | + | [[Category: Richard SB]] |
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Current revision
CRYSTAL STRUCTURE OF 4-DIPHOSPHOCYTIDYL-2-C-METHYLERYTHRITOL (CDP-ME) SYNTHASE (YGBP) INVOLVED IN MEVALONATE INDEPENDENT ISOPRENOID BIOSYNTHESIS
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Categories: Escherichia coli K-12 | Large Structures | Bowman ME | Cane DE | Chow C | Kang I | Kwiatkowski W | Lillo M | Noel JP | Richard SB