2abw: Difference between revisions
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New page: left|200px<br /><applet load="2abw" size="350" color="white" frame="true" align="right" spinBox="true" caption="2abw, resolution 1.620Å" /> '''Glutaminase subunit... |
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== | ==Glutaminase subunit of the plasmodial PLP synthase (Vitamin B6 biosynthesis)== | ||
Vitamin B6 is one of nature's most versatile cofactors. Most organisms | <StructureSection load='2abw' size='340' side='right'caption='[[2abw]], [[Resolution|resolution]] 1.62Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2abw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ABW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ABW FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.62Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></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=2abw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2abw OCA], [https://pdbe.org/2abw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2abw RCSB], [https://www.ebi.ac.uk/pdbsum/2abw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2abw ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PDX2_PLAF7 PDX2_PLAF7] Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of Pdx1.<ref>PMID:15590634</ref> <ref>PMID:16339145</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ab/2abw_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2abw ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Vitamin B6 is one of nature's most versatile cofactors. Most organisms synthesize vitamin B6 via a recently discovered pathway employing the proteins Pdx1 and Pdx2. Here we present an in-depth characterization of the respective orthologs from the malaria parasite, Plasmodium falciparum. Expression profiling of Pdx1 and -2 shows that blood-stage parasites indeed possess a functional vitamin B6 de novo biosynthesis. Recombinant Pdx1 and Pdx2 form a complex that functions as a glutamine amidotransferase with Pdx2 as the glutaminase and Pdx1 as pyridoxal-5 '-phosphate synthase domain. Complex formation is required for catalytic activity of either domain. Pdx1 forms a chimeric bi-enzyme with the bacterial YaaE, a Pdx2 ortholog, both in vivo and in vitro, although this chimera does not attain full catalytic activity, emphasizing that species-specific structural features govern the interaction between the protein partners of the PLP synthase complexes in different organisms. To gain insight into the activation mechanism of the parasite bi-enzyme complex, the three-dimensional structure of Pdx2 was determined at 1.62 A. The obstruction of the oxyanion hole indicates that Pdx2 is in a resting state and that activation occurs upon Pdx1-Pdx2 complex formation. | |||
Vitamin B6 biosynthesis by the malaria parasite Plasmodium falciparum: biochemical and structural insights.,Gengenbacher M, Fitzpatrick TB, Raschle T, Flicker K, Sinning I, Muller S, Macheroux P, Tews I, Kappes B J Biol Chem. 2006 Feb 10;281(6):3633-41. Epub 2005 Dec 8. PMID:16339145<ref>PMID:16339145</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2abw" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Plasmodium falciparum]] | [[Category: Plasmodium falciparum]] | ||
[[Category: Fitzpatrick TB]] | |||
[[Category: Fitzpatrick | [[Category: Flicker K]] | ||
[[Category: Flicker | [[Category: Gengenbacher M]] | ||
[[Category: Gengenbacher | [[Category: Kappes B]] | ||
[[Category: Kappes | [[Category: Macheroux P]] | ||
[[Category: Macheroux | [[Category: Mueller S]] | ||
[[Category: Mueller | [[Category: Raschle T]] | ||
[[Category: Raschle | [[Category: Sinning I]] | ||
[[Category: Sinning | [[Category: Tews I]] | ||
[[Category: Tews | |||
