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| | <StructureSection load='5xf2' size='340' side='right'caption='[[5xf2]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='5xf2' size='340' side='right'caption='[[5xf2]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xf2]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XF2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XF2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xf2]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei_K96243 Burkholderia pseudomallei K96243]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XF2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XF2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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]] 2.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5x9q|5x9q]]</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=5xf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xf2 OCA], [https://pdbe.org/5xf2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xf2 RCSB], [https://www.ebi.ac.uk/pdbsum/5xf2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xf2 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xf2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xf2 OCA], [http://pdbe.org/5xf2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xf2 RCSB], [http://www.ebi.ac.uk/pdbsum/5xf2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xf2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q63XZ4_BURPS Q63XZ4_BURPS]] Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.[SAAS:SAAS00558028] | + | [https://www.uniprot.org/uniprot/Q63XZ4_BURPS Q63XZ4_BURPS] Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.[SAAS:SAAS00558028] |
| | <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: Burkholderia pseudomallei K96243]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kim, H]] | + | [[Category: Kim H]] |
| - | [[Category: Kim, S]] | + | [[Category: Kim S]] |
| - | [[Category: Lee, D]] | + | [[Category: Lee D]] |
| - | [[Category: Park, J]] | + | [[Category: Park J]] |
| - | [[Category: Shin, D H]] | + | [[Category: Shin DH]] |
| - | [[Category: Burkholderia pseudomalle]]
| + | |
| - | [[Category: D-glycero-beta-d-manno-heptose-1-phosphate adenylyltransferase]]
| + | |
| - | [[Category: Hldc]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q63XZ4_BURPS Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.[SAAS:SAAS00558028]
Publication Abstract from PubMed
The Gram-negative bacterium Burkholderia pseudomallei is the causative agent of melioidosis. D-glycero-beta-D-manno-Heptose-1-phosphate adenylyltransferase (HldC) is the fourth enzyme of the ADP-L-glycero-beta-D-manno-heptose biosynthesis pathway, which produces an essential carbohydrate comprising the inner core of lipopolysaccharide. Therefore, HldC is a potential target of antibiotics against melioidosis. In this study, HldC from B. pseudomallei has been cloned, expressed, purified and crystallized. Synchrotron X-ray data from a selenomethionine-substituted HldC crystal were also collected to 2.8 A resolution. The crystal belonged to the primitive triclinic space group P1, with unit-cell parameters a = 74.0, b = 74.0, c = 74.9 A, alpha = 108.4, beta = 108.4, gamma = 108.0 degrees . Eight protomers are present in the unit cell and three out of five selenomethionines were found in each protomer using the PHENIX software suite. A full structural determination is in progress to elucidate the structure-function relationship of the protein.
Expression and crystallographic studies of D-glycero-beta-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei.,Park J, Kim H, Kim S, Lee D, Shin DH Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):90-94. doi:, 10.1107/S2053230X16020537. Epub 2017 Jan 19. PMID:28177319[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Park J, Kim H, Kim S, Lee D, Shin DH. Expression and crystallographic studies of D-glycero-beta-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei. Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):90-94. doi:, 10.1107/S2053230X16020537. Epub 2017 Jan 19. PMID:28177319 doi:http://dx.doi.org/10.1107/S2053230X16020537
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