3e04: Difference between revisions

Latest revision as of 12:56, 30 August 2023

Crystal structure of human fumarate hydratase

Structural highlights

3e04 is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.95Å
Ligands:	EDO
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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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

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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

[1]

[2]

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:3e04.jpg|left|200px]]
-<!--
+==Crystal structure of human fumarate hydratase==
-The line below this paragraph, containing "STRUCTURE_3e04", creates the "Structure Box" on the page.
+<StructureSection load='3e04' size='340' side='right'caption='[[3e04]], [[Resolution|resolution]] 1.95&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'>[[3e04]] is a 4 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=3E04 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E04 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]] 1.95&#8491;</td></tr>
--->
+<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></td></tr>
-{{STRUCTURE_3e04|  PDB=3e04  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3e04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e04 OCA], [https://pdbe.org/3e04 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e04 RCSB], [https://www.ebi.ac.uk/pdbsum/3e04 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e04 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[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 ==
+[https://www.uniprot.org/uniprot/FUMH_HUMAN FUMH_HUMAN] Also acts as a tumor suppressor.
+== 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/e0/3e04_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=3e04 ConSurf].
+<div style="clear:both"></div>
-===Crystal structure of human fumarate hydratase===
+==See Also==
+*[[Fumarase|Fumarase]]
+== References ==
-==Disease==
+<references/>
-Known disease associated with this structure: Fumarase deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=136850 136850]], Hypercholesterolemia, familial OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=606945 606945]], Leiomyomatosis and renal cell cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=136850 136850]], Multiple cutaneous and uterine leiomyomata OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=136850 136850]]
+__TOC__
+</StructureSection>
-==About this Structure==
-E04 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E04 OCA].
-[[Category: Fumarate hydratase]]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Kavanagh, K L.]]
+[[Category: Kavanagh KL]]
-[[Category: Oppermann, U.]]
+[[Category: Oppermann U]]
-[[Category: SGC, Structural Genomics Consortium.]]
-[[Category: Acetylation]]
-[[Category: Alternative initiation]]
-[[Category: Anti-oncogene]]
-[[Category: Cell cycle]]
-[[Category: Cytoplasm]]
-[[Category: Disease mutation]]
-[[Category: Fumarase]]
-[[Category: Lyase]]
-[[Category: Mitochondrion]]
-[[Category: Sgc]]
-[[Category: Structural genomics consortium]]
-[[Category: Tca cycle]]
-[[Category: Transit peptide]]
-[[Category: Tricarboxylic acid cycle]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 13 14:45:20 2008''

3e04: Difference between revisions

Latest revision as of 12:56, 30 August 2023

Crystal structure of human fumarate hydratase

Structural highlights

Disease

Function

Evolutionary Conservation

See Also

References

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