5x9q: Difference between revisions

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'''Unreleased structure'''


The entry 5x9q is ON HOLD  until Paper Publication
==Crystal structure of HldC from Burkholderia pseudomallei==
<StructureSection load='5x9q' size='340' side='right' caption='[[5x9q]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5x9q]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X9Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X9Q FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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=5x9q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x9q OCA], [http://pdbe.org/5x9q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x9q RCSB], [http://www.ebi.ac.uk/pdbsum/5x9q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x9q 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 crystal structure of HldC from B. pseudomallei (BpHldC), the fourth enzyme of the heptose biosynthesis pathway, has been determined. BpHldC converts ATP and d-glycero-beta-d-manno-heptose-1-phosphate into ADP-d-glycero-beta-d-manno-heptose and pyrophosphate. The crystal structure of BpHldC belongs to the nucleotidyltransferase alpha/beta phosphodiesterase superfamily sharing a common Rossmann-like alpha/beta fold with a conserved T/HXGH sequence motif. The invariant catalytic key residues of BpHldC indicate that the core catalytic mechanism of BpHldC may be similar to that of other closest homologues. Intriguingly, a reorientation of the C-terminal helix seems to guide open and close states of the active site for the catalytic reaction.


Authors: Park, J., Kim, H., Kim, S., Lee, D., Shin, D.H.
Crystal structure of D-glycero-Beta-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei.,Park J, Kim H, Kim S, Lee D, Kim MS, Shin DH Proteins. 2018 Jan;86(1):124-131. doi: 10.1002/prot.25398. Epub 2017 Oct 31. PMID:28986923<ref>PMID:28986923</ref>


Description: Crystal structure of HldC from Burkholderia pseudomallei
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Park, J]]
<div class="pdbe-citations 5x9q" 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: Shin, D.H]]
[[Category: Park, J]]
[[Category: Kim, S]]
[[Category: Shin, D H]]
[[Category: D-glycero-beta-d-manno-heptose-1-phosphate adenylyltransferase]]
[[Category: Heptose biosynthesis pathway]]
[[Category: Hldc]]
[[Category: Hlde2]]
[[Category: Transferase]]
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