5d6b: Difference between revisions

Revision as of 10:23, 21 June 2023

Human fumarase (wild type)

Structural highlights

5d6b is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

FUMH_HUMAN Defects in FH are the cause of fumarase deficiency (FHD) [MIM:606812; also known as fumaricaciduria. FHD is characterized by progressive encephalopathy, developmental delay, hypotonia, cerebral atrophy and lactic and pyruvic acidemia.[:]^[1] Defects in FH are the cause of hereditary leiomyomatosis and renal cell cancer (HLRCC) [MIM:150800. A disorder characterized by predisposition to cutaneous and uterine leiomyomas, and papillary type 2 renal cancer which occurs in about 20% of patients.^[2]

Function

FUMH_HUMAN Also acts as a tumor suppressor.

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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Coughlin EM, Christensen E, Kunz PL, Krishnamoorthy KS, Walker V, Dennis NR, Chalmers RA, Elpeleg ON, Whelan D, Pollitt RJ, Ramesh V, Mandell R, Shih VE. Molecular analysis and prenatal diagnosis of human fumarase deficiency. Mol Genet Metab. 1998 Apr;63(4):254-62. PMID:9635293 doi:S1096-7192(98)92684-1
↑ Tomlinson IP, Alam NA, Rowan AJ, Barclay E, Jaeger EE, Kelsell D, Leigh I, Gorman P, Lamlum H, Rahman S, Roylance RR, Olpin S, Bevan S, Barker K, Hearle N, Houlston RS, Kiuru M, Lehtonen R, Karhu A, Vilkki S, Laiho P, Eklund C, Vierimaa O, Aittomaki K, Hietala M, Sistonen P, Paetau A, Salovaara R, Herva R, Launonen V, Aaltonen LA. Germline mutations in FH predispose to dominantly inherited uterine fibroids, skin leiomyomata and papillary renal cell cancer. Nat Genet. 2002 Apr;30(4):406-10. Epub 2002 Feb 25. PMID:11865300 doi:10.1038/ng849
↑ Pereira de Padua RA, Nonato MC. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of recombinant human fumarase. Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):120-2. doi:, 10.1107/S2053230X13033955. Epub 2013 Dec 24. PMID:24419633 doi:https://dx.doi.org/10.1107/S2053230X13033955

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Coughlin EM, Christensen E, Kunz PL, Krishnamoorthy KS, Walker V, Dennis NR, Chalmers RA, Elpeleg ON, Whelan D, Pollitt RJ, Ramesh V, Mandell R, Shih VE. Molecular analysis and prenatal diagnosis of human fumarase deficiency. Mol Genet Metab. 1998 Apr;63(4):254-62. PMID:9635293 doi:S1096-7192(98)92684-1

[2] Tomlinson IP, Alam NA, Rowan AJ, Barclay E, Jaeger EE, Kelsell D, Leigh I, Gorman P, Lamlum H, Rahman S, Roylance RR, Olpin S, Bevan S, Barker K, Hearle N, Houlston RS, Kiuru M, Lehtonen R, Karhu A, Vilkki S, Laiho P, Eklund C, Vierimaa O, Aittomaki K, Hietala M, Sistonen P, Paetau A, Salovaara R, Herva R, Launonen V, Aaltonen LA. Germline mutations in FH predispose to dominantly inherited uterine fibroids, skin leiomyomata and papillary renal cell cancer. Nat Genet. 2002 Apr;30(4):406-10. Epub 2002 Feb 25. PMID:11865300 doi:10.1038/ng849

[3] Pereira de Padua RA, Nonato MC. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of recombinant human fumarase. Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):120-2. doi:, 10.1107/S2053230X13033955. Epub 2013 Dec 24. PMID:24419633 doi:https://dx.doi.org/10.1107/S2053230X13033955

[1]

[2]

[3]

@@ Line 3: / Line 3: @@
 <StructureSection load='5d6b' size='340' side='right'caption='[[5d6b]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5d6b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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>
+<table><tr><td colspan='2'>[[5d6b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5D6B FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</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=5d6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5d6b OCA], [https://pdbe.org/5d6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5d6b RCSB], [https://www.ebi.ac.uk/pdbsum/5d6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5d6b ProSAT]</span></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>
+[https://www.uniprot.org/uniprot/FUMH_HUMAN FUMH_HUMAN] Defects in FH are the cause of fumarase deficiency (FHD) [MIM:[https://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:[https://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.
+[https://www.uniprot.org/uniprot/FUMH_HUMAN FUMH_HUMAN] Also acts as a tumor suppressor.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 28: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Fumarate hydratase]]
+[[Category: Homo sapiens]]
-[[Category: Human]]
 [[Category: Large Structures]]
-[[Category: Nonato, M C]]
+[[Category: Nonato MC]]
-[[Category: Padua, R A.Pereira de]]
+[[Category: Pereira de Padua RA]]
-[[Category: Lyase]]
-[[Category: Tca cycle]]

5d6b: Difference between revisions

Revision as of 10:23, 21 June 2023

Human fumarase (wild type)

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

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