6dsr

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m (Protected "6dsr" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6dsr is ON HOLD
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==Re-refinement of P. falciparum orotidine 5'-monophosphate decarboxylase==
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<StructureSection load='6dsr' size='340' side='right' caption='[[6dsr]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6dsr]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DSR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DSR FirstGlance]. <br>
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</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>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2za1|2za1]]</td></tr>
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<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>
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<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=6dsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dsr OCA], [http://pdbe.org/6dsr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dsr RCSB], [http://www.ebi.ac.uk/pdbsum/6dsr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dsr ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Brandt, G.S., Novak, W.R.P.
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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>
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Description: Re-refinement of P. falciparum orotidine 5'-monophosphate decarboxylase
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Novak, W.R.P]]
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<div class="pdbe-citations 6dsr" style="background-color:#fffaf0;"></div>
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[[Category: Brandt, G.S]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Orotidine-5'-phosphate decarboxylase]]
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[[Category: Brandt, G S]]
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[[Category: Novak, W R.P]]
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[[Category: Complex]]
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[[Category: Lyase]]
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[[Category: P falciparum]]

Revision as of 07:58, 17 October 2018

Re-refinement of P. falciparum orotidine 5'-monophosphate decarboxylase

6dsr, resolution 2.60Å

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