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| | <StructureSection load='2xwl' size='340' side='right'caption='[[2xwl]], [[Resolution|resolution]] 1.49Å' scene=''> | | <StructureSection load='2xwl' size='340' side='right'caption='[[2xwl]], [[Resolution|resolution]] 1.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xwl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_smegmatis"_trevisan_1889 "bacillus smegmatis" trevisan 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XWL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xwl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XWL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XWL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.49Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2xwn|2xwn]], [[2xwm|2xwm]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CTP:CYTIDINE-5-TRIPHOSPHATE'>CTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/2-C-methyl-D-erythritol_4-phosphate_cytidylyltransferase 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.60 2.7.7.60] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xwl OCA], [https://pdbe.org/2xwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xwl RCSB], [https://www.ebi.ac.uk/pdbsum/2xwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xwl ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xwl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xwl OCA], [https://pdbe.org/2xwl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xwl RCSB], [https://www.ebi.ac.uk/pdbsum/2xwl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xwl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/A0R560_MYCS2 A0R560_MYCS2]] Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (By similarity).[SAAS:SAAS018294_004_010899][HAMAP-Rule:MF_00108]
| + | [https://www.uniprot.org/uniprot/A0R560_MYCS2 A0R560_MYCS2] Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (By similarity).[SAAS:SAAS018294_004_010899][HAMAP-Rule:MF_00108] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus smegmatis trevisan 1889]] | |
| - | [[Category: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bergfors, T]] | + | [[Category: Mycolicibacterium smegmatis]] |
| - | [[Category: Bjorkelid, C]] | + | [[Category: Bergfors T]] |
| - | [[Category: Jones, T A]]
| + | [[Category: Bjorkelid C]] |
| - | [[Category: Unge, T]] | + | [[Category: Jones TA]] |
| - | [[Category: Mep pathway]] | + | [[Category: Unge T]] |
| - | [[Category: Transferase]] | + | |
| Structural highlights
Function
A0R560_MYCS2 Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (By similarity).[SAAS:SAAS018294_004_010899][HAMAP-Rule:MF_00108]
Publication Abstract from PubMed
A number of pathogens, including the causative agents of tuberculosis and malaria, synthesize isopentenyl diphosphate via the 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway rather than the classical mevalonate pathway found in humans. As part of a structure-based drug-discovery program against tuberculosis, IspD, the enzyme that carries out the third step in the MEP pathway, was targeted. Constructs of both the Mycobacterium smegmatis and the Mycobacterium tuberculosis enzymes that were suitable for structural and inhibitor-screening studies were engineered. Two crystal structures of the M. smegmatis enzyme were produced, one in complex with CTP and the other in complex with CMP. In addition, the M. tuberculosis enzyme was crystallized in complex with CTP. Here, the structure determination and crystallographic refinement of these crystal forms and the enzymatic characterization of the M. tuberculosis enzyme construct are reported. A comparison with known IspD structures allowed the definition of the structurally conserved core of the enzyme. It indicates potential flexibility in the enzyme and in particular in areas close to the active site. These well behaved constructs provide tools for future target-based screening of potential inhibitors. The conserved nature of the extended active site suggests that any new inhibitor will potentially exhibit broad-spectrum activity.
Structural and functional studies of mycobacterial IspD enzymes.,Bjorkelid C, Bergfors T, Henriksson LM, Stern AL, Unge T, Mowbray SL, Jones TA Acta Crystallogr D Biol Crystallogr. 2011 May;67(Pt 5):403-14. Epub 2011, Apr 8. PMID:21543842[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bjorkelid C, Bergfors T, Henriksson LM, Stern AL, Unge T, Mowbray SL, Jones TA. Structural and functional studies of mycobacterial IspD enzymes. Acta Crystallogr D Biol Crystallogr. 2011 May;67(Pt 5):403-14. Epub 2011, Apr 8. PMID:21543842 doi:10.1107/S0907444911006160
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