5l2r
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5l2r is ON HOLD Authors: Feliciano, P.R., Drennan, C.L., Nonato, M.C. Description: Crystal structure of fumarate hydratase from Leishmania major [[...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of fumarate hydratase from Leishmania major== | |
| + | <StructureSection load='5l2r' size='340' side='right'caption='[[5l2r]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5l2r]] 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=5L2R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5L2R 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]] 2.054Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LMR:(2S)-2-HYDROXYBUTANEDIOIC+ACID'>LMR</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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=5l2r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l2r OCA], [https://pdbe.org/5l2r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5l2r RCSB], [https://www.ebi.ac.uk/pdbsum/5l2r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5l2r ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/FUM2_LEIMA FUM2_LEIMA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Fumarate hydratases (FHs) are essential metabolic enzymes grouped into two classes. Here, we present the crystal structure of a class I FH, the cytosolic FH from Leishmania major, which reveals a previously undiscovered protein fold that coordinates a catalytically essential [4Fe-4S] cluster. Our 2.05 A resolution data further reveal a dimeric architecture for this FH that resembles a heart, with each lobe comprised of two domains that are arranged around the active site. Besides the active site, where the substrate S-malate is bound bidentate to the unique iron of the [4Fe-4S] cluster, other binding pockets are found near the dimeric enzyme interface, some of which are occupied by malonate, shown here to be a weak inhibitor of this enzyme. Taken together, these data provide a framework both for investigations of the class I FH catalytic mechanism and for drug design aimed at fighting neglected tropical diseases. | ||
| - | + | Crystal structure of an Fe-S cluster-containing fumarate hydratase enzyme from Leishmania major reveals a unique protein fold.,Feliciano PR, Drennan CL, Nonato MC Proc Natl Acad Sci U S A. 2016 Aug 30;113(35):9804-9. doi:, 10.1073/pnas.1605031113. Epub 2016 Aug 15. PMID:27528683<ref>PMID:27528683</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5l2r" style="background-color:#fffaf0;"></div> |
| - | [[Category: Drennan | + | == References == |
| - | [[Category: Feliciano | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Leishmania major]] | ||
| + | [[Category: Drennan CL]] | ||
| + | [[Category: Feliciano PR]] | ||
| + | [[Category: Nonato MC]] | ||
Current revision
Crystal structure of fumarate hydratase from Leishmania major
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