5xf2: Difference between revisions
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==Crystal structure of SeMet-HldC from Burkholderia pseudomallei== | |||
<StructureSection load='5xf2' size='340' side='right' caption='[[5xf2]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XF2 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></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='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'>[http://oca.weizmann.ac.il/oca-docs/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> | |||
== 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] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:28177319</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5xf2" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Kim, H]] | [[Category: Kim, H]] | ||
[[Category: Kim, S]] | |||
[[Category: Lee, D]] | [[Category: Lee, D]] | ||
[[Category: Park, J]] | [[Category: Park, J]] | ||
[[Category: Shin, D H]] | |||
[[Category: Burkholderia pseudomalle]] | |||
[[Category: D-glycero-beta-d-manno-heptose-1-phosphate adenylyltransferase]] | |||
[[Category: Hldc]] | |||
[[Category: Transferase]] | |||
Revision as of 16:24, 20 October 2017
Crystal structure of SeMet-HldC from Burkholderia pseudomallei
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