1e7w

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[[Image:1e7w.png|left|200px]]
 
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==One active site, two modes of reduction correlate the mechanism of leishmania pteridine reductase with pterin metabolism and antifolate drug resistance in trpanosomes==
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The line below this paragraph, containing "STRUCTURE_1e7w", creates the "Structure Box" on the page.
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<StructureSection load='1e7w' size='340' side='right'caption='[[1e7w]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1e7w]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E7W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E7W FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MTX:METHOTREXATE'>MTX</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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{{STRUCTURE_1e7w| PDB=1e7w | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e7w OCA], [https://pdbe.org/1e7w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e7w RCSB], [https://www.ebi.ac.uk/pdbsum/1e7w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e7w ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PTR1_LEIMA PTR1_LEIMA] Exhibits a NADPH-dependent biopterin reductase activity. Has good activity with folate and significant activity with dihydrofolate and dihydrobiopterin, but not with quinonoid dihydrobiopterin. Confers resistance to methotrexate (MTX).<ref>PMID:7972081</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e7/1e7w_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1e7w ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Pteridine reductase (PTR1) is a short-chain reductase (SDR) responsible for the salvage of pterins in parasitic trypanosomatids. PTR1 catalyzes the NADPH-dependent two-step reduction of oxidized pterins to the active tetrahydro-forms and reduces susceptibility to antifolates by alleviating dihydrofolate reductase (DHFR) inhibition. Crystal structures of PTR1 complexed with cofactor and 7,8-dihydrobiopterin (DHB) or methotrexate (MTX) delineate the enzyme mechanism, broad spectrum of activity and inhibition by substrate or an antifolate. PTR1 applies two distinct reductive mechanisms to substrates bound in one orientation. The first reduction uses the generic SDR mechanism, whereas the second shares similarities with the mechanism proposed for DHFR. Both DHB and MTX form extensive hydrogen bonding networks with NADP(H) but differ in the orientation of the pteridine.
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===ONE ACTIVE SITE, TWO MODES OF REDUCTION CORRELATE THE MECHANISM OF LEISHMANIA PTERIDINE REDUCTASE WITH PTERIN METABOLISM AND ANTIFOLATE DRUG RESISTANCE IN TRPANOSOMES===
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Pteridine reductase mechanism correlates pterin metabolism with drug resistance in trypanosomatid parasites.,Gourley DG, Schuttelkopf AW, Leonard GA, Luba J, Hardy LW, Beverley SM, Hunter WN Nat Struct Biol. 2001 Jun;8(6):521-5. PMID:11373620<ref>PMID:11373620</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1e7w" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11373620}}, adds the Publication Abstract to the page
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*[[Pteridine reductase|Pteridine reductase]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11373620 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11373620}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[1e7w]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_major Leishmania major]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E7W OCA].
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==Reference==
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<ref group="xtra">PMID:011373620</ref><ref group="xtra">PMID:012925782</ref><references group="xtra"/>
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[[Category: Leishmania major]]
[[Category: Leishmania major]]
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[[Category: Pteridine reductase]]
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[[Category: Gourley DG]]
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[[Category: Gourley, D G.]]
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[[Category: Hunter WN]]
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[[Category: Hunter, W N.]]
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[[Category: Dihydrofolate reductase]]
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[[Category: Methotrexate resistance]]
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[[Category: Oxidoreductase]]
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[[Category: Pteridine reductase]]
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[[Category: Shortchain dehydrogenase]]
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Current revision

One active site, two modes of reduction correlate the mechanism of leishmania pteridine reductase with pterin metabolism and antifolate drug resistance in trpanosomes

PDB ID 1e7w

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