3lg0: Difference between revisions

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-[[Image:3lg0.png|left|200px]]
-<!--
+==Structure of Plasmodium falciparum ornithine delta-aminotransferase==
-The line below this paragraph, containing "STRUCTURE_3lg0", creates the "Structure Box" on the page.
+<StructureSection load='3lg0' size='340' side='right'caption='[[3lg0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3lg0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_CDC/Honduras Plasmodium falciparum CDC/Honduras]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LG0 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</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=3lg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lg0 OCA], [https://pdbe.org/3lg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lg0 RCSB], [https://www.ebi.ac.uk/pdbsum/3lg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lg0 ProSAT]</span></td></tr>
-{{STRUCTURE_3lg0|  PDB=3lg0  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/OAT_PLAF7 OAT_PLAF7] The enzyme has a very narrow substrate specificity and can only catalyze the transamination of alpha-ketoglutarate with ornithine or N-acetylornithine and of glutamate-5-semialdehyde with glutamate and alanine.
+== 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/lg/3lg0_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=3lg0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Ornithine delta-aminotransferase (OAT) of the malaria parasite Plasmodium falciparum catalyzes the reversible conversion of ornithine into glutamate-5-semialdehyde and glutamate and is-in contrast to its human counterpart-activated by thioredoxin (Trx) by a factor of 10. Trx, glutaredoxin, and plasmoredoxin are redox-active proteins that play a crucial role in the maintenance and control of redox reactions, and were shown to interact with P. falciparum OAT. OAT, which is involved in ornithine homeostasis and proline biosynthesis, is essential for mitotic cell division in rapidly growing cells, thus representing a potential target for chemotherapeutic intervention. Here we report the three-dimensional crystal structure of P. falciparum OAT at 2.3 A resolution. The overall structure is very similar to that of the human OAT. However, in plasmodial OAT, the loop involved in substrate binding contains two cysteine residues, which are lacking in human OAT. Site-directed mutagenesis of these cysteines and functional analysis demonstrated that Cys154 and Cys163 mediate the interaction with Trx. Interestingly, the Cys154--&gt;Ser mutant has a strongly reduced specific activity, most likely due to impaired binding of ornithine. Cys154 and Cys163 are highly conserved in Plasmodium but do not exist in other organisms, suggesting that redox regulation of OAT by Trx is specific for malaria parasites. Plasmodium might require a tight Trx-mediated control of OAT activity for coordinating ornithine homeostasis, polyamine synthesis, proline synthesis, and mitotic cell division.
-===Structure of Plasmodium falciparum ornithine delta-aminotransferase===
+Redox regulation of Plasmodium falciparum ornithine delta-aminotransferase.,Jortzik E, Fritz-Wolf K, Sturm N, Hipp M, Rahlfs S, Becker K J Mol Biol. 2010 Sep 17;402(2):445-59. Epub 2010 Jul 29. PMID:20673832<ref>PMID:20673832</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_20673832}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3lg0" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 20673832 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20673832}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-[[3lg0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LG0 OCA].
+[[Category: Plasmodium falciparum CDC/Honduras]]
+[[Category: Becker K]]
-==Reference==
+[[Category: Fritz-Wolf K]]
-<ref group="xtra">PMID:20673832</ref><references group="xtra"/>
+[[Category: Jortzik E]]
-[[Category: Ornithine aminotransferase]]
+[[Category: Stumpf M]]
-[[Category: Plasmodium falciparum]]
-[[Category: Becker, K.]]
-[[Category: Fritz-Wolf, K.]]
-[[Category: Jortzik, E.]]
-[[Category: Stumpf, M.]]