4a35: Difference between revisions
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== | |||
<StructureSection load='4a35' size='340' side='right' caption='[[4a35]], [[Resolution|resolution]] 1.74Å' scene=''> | ==Crystal structure of human Mitochondrial enolase superfamily member 1 (ENOSF1)== | ||
<StructureSection load='4a35' size='340' side='right'caption='[[4a35]], [[Resolution|resolution]] 1.74Å' scene=''> | |||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a35]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4a35]] 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=4A35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A35 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.74Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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=MG:MAGNESIUM+ION'>MG</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=4a35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a35 OCA], [https://pdbe.org/4a35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a35 RCSB], [https://www.ebi.ac.uk/pdbsum/4a35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a35 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ENOF1_HUMAN ENOF1_HUMAN] May regulate thymidylate synthase activity.<ref>PMID:8869746</ref> <ref>PMID:14508106</ref> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In humans, the gene encoding a reverse thymidylate synthase (rTS) is transcribed in the reverse direction of the gene encoding thymidylate synthase (TS) that is involved in DNA biosynthesis. Three isoforms are found: alpha, beta, and gamma, with the transcript of the alpha-isoform overlapping with that of TS. rTSbeta has been of interest since the discovery of its overexpression in methotrexate and 5-fluorouracil resistant cell lines. Despite more than 20 years of study, none of the rTS isoforms have been biochemically or structurally characterized. In this study, we identified rTSgamma as an l-fuconate dehydratase and determined its high-resolution crystal structure. Our data provide an explanation for the observed difference in enzymatic activities between rTSbeta and rTSgamma, enabling more informed proposals for the possible function of rTSbeta in chemotherapeutic resistance. | |||
Enzymatic and structural characterization of rTSgamma provides insights into the function of rTSbeta.,Wichelecki DJ, Froese DS, Kopec J, Muniz JR, Yue WW, Gerlt JA Biochemistry. 2014 Apr 29;53(16):2732-8. doi: 10.1021/bi500349e. Epub 2014 Apr, 15. PMID:24697329<ref>PMID:24697329</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4a35" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Enolase 3D structures|Enolase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Arrowsmith CH]] | ||
[[Category: | [[Category: Bountra C]] | ||
[[Category: | [[Category: Canning P]] | ||
[[Category: Edwards | [[Category: Edwards AM]] | ||
[[Category: Froese | [[Category: Froese DS]] | ||
[[Category: Krojer | [[Category: Krojer T]] | ||
[[Category: Muniz | [[Category: Muniz JRC]] | ||
[[Category: Oppermann | [[Category: Oppermann U]] | ||
[[Category: Vollmar | [[Category: Vollmar M]] | ||
[[Category: Weigelt | [[Category: Weigelt J]] | ||
[[Category: Yue | [[Category: Yue WW]] | ||
[[Category: | [[Category: Von Delft F]] | ||
Latest revision as of 13:45, 9 May 2024
Crystal structure of human Mitochondrial enolase superfamily member 1 (ENOSF1)Crystal structure of human Mitochondrial enolase superfamily member 1 (ENOSF1)
Structural highlights
FunctionENOF1_HUMAN May regulate thymidylate synthase activity.[1] [2] Publication Abstract from PubMedIn humans, the gene encoding a reverse thymidylate synthase (rTS) is transcribed in the reverse direction of the gene encoding thymidylate synthase (TS) that is involved in DNA biosynthesis. Three isoforms are found: alpha, beta, and gamma, with the transcript of the alpha-isoform overlapping with that of TS. rTSbeta has been of interest since the discovery of its overexpression in methotrexate and 5-fluorouracil resistant cell lines. Despite more than 20 years of study, none of the rTS isoforms have been biochemically or structurally characterized. In this study, we identified rTSgamma as an l-fuconate dehydratase and determined its high-resolution crystal structure. Our data provide an explanation for the observed difference in enzymatic activities between rTSbeta and rTSgamma, enabling more informed proposals for the possible function of rTSbeta in chemotherapeutic resistance. Enzymatic and structural characterization of rTSgamma provides insights into the function of rTSbeta.,Wichelecki DJ, Froese DS, Kopec J, Muniz JR, Yue WW, Gerlt JA Biochemistry. 2014 Apr 29;53(16):2732-8. doi: 10.1021/bi500349e. Epub 2014 Apr, 15. PMID:24697329[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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