6dss: Difference between revisions

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'''Unreleased structure'''


The entry 6dss is ON HOLD
==Re-refinement of P. falciparum orotidine 5'-monophosphate decarboxylase==
<StructureSection load='6dss' size='340' side='right' caption='[[6dss]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6dss]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DSS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DSS FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=U5P:URIDINE-5-MONOPHOSPHATE'>U5P</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2za3|2za3]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] </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=6dss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dss OCA], [http://pdbe.org/6dss PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dss RCSB], [http://www.ebi.ac.uk/pdbsum/6dss PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dss ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Orotidine 5'-monophoshate decarboxylase (OMPDC) catalyses the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). Here, we report the X-ray analysis of apo, substrate or product-complex forms of OMPDC from Plasmodium falciparum (PfOMPDC) at 2.7, 2.65 and 2.65 A, respectively. The structural analysis provides the substrate recognition mechanism with dynamic structural changes, as well as the rearrangement of the hydrogen bond array at the active site. The structural basis of substrate or product binding to PfOMPDC will help to uncover the decarboxylation mechanism and facilitate structure-based optimization of antimalarial drugs.


Authors: Brandt, G.S., Novak, W.R.P.
Structural basis for the decarboxylation of orotidine 5'-monophosphate (OMP) by Plasmodium falciparum OMP decarboxylase.,Tokuoka K, Kusakari Y, Krungkrai SR, Matsumura H, Kai Y, Krungkrai J, Horii T, Inoue T J Biochem. 2008 Jan;143(1):69-78. Epub 2007 Nov 1. PMID:17981823<ref>PMID:17981823</ref>


Description: Re-refinement of P. falciparum orotidine 5'-monophosphate decarboxylase
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Novak, W.R.P]]
<div class="pdbe-citations 6dss" style="background-color:#fffaf0;"></div>
[[Category: Brandt, G.S]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Orotidine-5'-phosphate decarboxylase]]
[[Category: Brandt, G S]]
[[Category: Novak, W R.P]]
[[Category: Complex]]
[[Category: Lyase]]
[[Category: P falciparum]]
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