5d6b
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Human fumarase (wild type)== | |
| + | <StructureSection load='5d6b' size='340' side='right' caption='[[5d6b]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5d6b]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5D6B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5D6B FirstGlance]. <br> | ||
| + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fumarate_hydratase Fumarate hydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.2 4.2.1.2] </span></td></tr> | ||
| + | <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=5d6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d6b OCA], [http://pdbe.org/5d6b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5d6b RCSB], [http://www.ebi.ac.uk/pdbsum/5d6b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5d6b ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/FUMH_HUMAN FUMH_HUMAN]] Defects in FH are the cause of fumarase deficiency (FHD) [MIM:[http://omim.org/entry/606812 606812]]; also known as fumaricaciduria. FHD is characterized by progressive encephalopathy, developmental delay, hypotonia, cerebral atrophy and lactic and pyruvic acidemia.[:]<ref>PMID:9635293</ref> Defects in FH are the cause of hereditary leiomyomatosis and renal cell cancer (HLRCC) [MIM:[http://omim.org/entry/150800 150800]]. A disorder characterized by predisposition to cutaneous and uterine leiomyomas, and papillary type 2 renal cancer which occurs in about 20% of patients.<ref>PMID:11865300</ref> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/FUMH_HUMAN FUMH_HUMAN]] Also acts as a tumor suppressor. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Human fumarase (HsFH) is a well-known citric acid cycle enzyme and is therefore a key component in energy metabolism. Genetic studies on human patients have shown that polymorphisms in the fumarase gene are responsible for diseases such as hereditary leiomyomatosis and renal cell cancer. As a first step in unravelling the molecular basis of the mechanism of fumarase deficiency in genetic disorders, the HsFH gene was cloned in pET-28a, heterologously expressed in Escherichia coli, purified by nickel-affinity chromatography and crystallized using the vapour-diffusion technique. X-ray diffraction experiments were performed at a synchrotron source and the structure was solved at 2.1 A resolution by molecular replacement. | ||
| - | + | Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of recombinant human fumarase.,Pereira de Padua RA, Nonato MC Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):120-2. doi:, 10.1107/S2053230X13033955. Epub 2013 Dec 24. PMID:24419633<ref>PMID:24419633</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5d6b" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Fumarate hydratase]] | ||
| + | [[Category: Nonato, M C]] | ||
| + | [[Category: Padua, R A.Pereira de]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Tca cycle]] | ||
Revision as of 06:49, 10 September 2016
Human fumarase (wild type)
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