1uek
From Proteopedia
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| - | [[ | + | ==Crystal structure of 4-(cytidine 5'-diphospho)-2C-methyl-D-erythritol kinase== |
| - | + | <StructureSection load='1uek' size='340' side='right' caption='[[1uek]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | < | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[1uek]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UEK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UEK FirstGlance]. <br> | |
| - | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ychB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 "Flavobacterium thermophilum" Yoshida and Oshima 1971])</td></tr> | |
| - | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-(cytidine_5'-diphospho)-2-C-methyl-D-erythritol_kinase 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.148 2.7.1.148] </span></td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uek FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uek OCA], [http://pdbe.org/1uek PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uek RCSB], [http://www.ebi.ac.uk/pdbsum/1uek PDBsum], [http://www.topsan.org/Proteins/RSGI/1uek TOPSAN]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [[http://www.uniprot.org/uniprot/ISPE_THET8 ISPE_THET8]] Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol.<ref>PMID:12771135</ref> | |
| - | ''' | + | == Evolutionary Conservation == |
| - | + | [[Image:Consurf_key_small.gif|200px|right]] | |
| - | + | Check<jmol> | |
| - | == | + | <jmolCheckbox> |
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ue/1uek_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
The crystal structure of the enzyme 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol (CDP-ME) kinase from the thermophilic bacterium Thermus thermophilus HB8 has been determined at 1.7-A resolution. This enzyme catalyzes phosphorylation of the 2-hydroxyl group of CDP-ME, the fourth step of the non-mevalonate pathway, which is essential for isoprenoid biosynthesis in several pathogenic microorganisms. Since this pathway is absent in humans, it is an important target for the development of novel antimicrobial compounds. The structure of the enzyme is similar to the structures of mevalonate kinase and homoserine kinase, members of the GHMP superfamily. Lys8 and Asp125 are active site residues in mevalonate kinase that also appear to play a catalytic role in CDP-ME kinase. Both the mevalonate and the non-mevalonate pathways therefore involve closely related kinases with similar mechanisms. Assaying the enzyme showed that CDP-ME kinase will phosphorylate CDP-ME but not 4-(uridine 5'-diphospho)-2-C-methyl-D-erythritol, indicating the substrate pyrimidine moiety is involved in important interactions with the enzyme. | The crystal structure of the enzyme 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol (CDP-ME) kinase from the thermophilic bacterium Thermus thermophilus HB8 has been determined at 1.7-A resolution. This enzyme catalyzes phosphorylation of the 2-hydroxyl group of CDP-ME, the fourth step of the non-mevalonate pathway, which is essential for isoprenoid biosynthesis in several pathogenic microorganisms. Since this pathway is absent in humans, it is an important target for the development of novel antimicrobial compounds. The structure of the enzyme is similar to the structures of mevalonate kinase and homoserine kinase, members of the GHMP superfamily. Lys8 and Asp125 are active site residues in mevalonate kinase that also appear to play a catalytic role in CDP-ME kinase. Both the mevalonate and the non-mevalonate pathways therefore involve closely related kinases with similar mechanisms. Assaying the enzyme showed that CDP-ME kinase will phosphorylate CDP-ME but not 4-(uridine 5'-diphospho)-2-C-methyl-D-erythritol, indicating the substrate pyrimidine moiety is involved in important interactions with the enzyme. | ||
| - | + | Crystal structure of 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase, an enzyme in the non-mevalonate pathway of isoprenoid synthesis.,Wada T, Kuzuyama T, Satoh S, Kuramitsu S, Yokoyama S, Unzai S, Tame JR, Park SY J Biol Chem. 2003 Aug 8;278(32):30022-7. Epub 2003 May 27. PMID:12771135<ref>PMID:12771135</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1uek" style="background-color:#fffaf0;"></div> |
| - | + | == References == | |
| - | [[Category: Kuramitsu, S | + | <references/> |
| - | [[Category: Park, S Y | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| - | [[Category: Tame, J R.H | + | [[Category: Flavobacterium thermophilum yoshida and oshima 1971]] |
| - | [[Category: Wada, T | + | [[Category: Kuramitsu, S]] |
| - | [[Category: Yokoyama, S | + | [[Category: Park, S Y]] |
| + | [[Category: Structural genomic]] | ||
| + | [[Category: Tame, J R.H]] | ||
| + | [[Category: Wada, T]] | ||
| + | [[Category: Yokoyama, S]] | ||
[[Category: Ghmp superfamily]] | [[Category: Ghmp superfamily]] | ||
[[Category: Non-mevalonate pathway]] | [[Category: Non-mevalonate pathway]] | ||
| - | [[Category: Riken structural genomics/proteomics initiative]] | ||
[[Category: Rsgi]] | [[Category: Rsgi]] | ||
| - | [[Category: | + | [[Category: Transferase]] |
| - | + | ||
Current revision
Crystal structure of 4-(cytidine 5'-diphospho)-2C-methyl-D-erythritol kinase
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