4gtl: Difference between revisions
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==T. Maritima FDTS (R174K mutant) with FAD== | ==T. Maritima FDTS (R174K mutant) with FAD== | ||
<StructureSection load='4gtl' size='340' side='right' caption='[[4gtl]], [[Resolution|resolution]] 2.17Å' scene=''> | <StructureSection load='4gtl' size='340' side='right'caption='[[4gtl]], [[Resolution|resolution]] 2.17Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4gtl]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4gtl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GTL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=4gtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gtl OCA], [https://pdbe.org/4gtl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gtl RCSB], [https://www.ebi.ac.uk/pdbsum/4gtl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gtl ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/THYX_THEMA THYX_THEMA] Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4gtl" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4gtl" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Thymidylate synthase 3D structures|Thymidylate synthase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermotoga maritima MSB8]] | ||
[[Category: | [[Category: Kohen A]] | ||
[[Category: | [[Category: Lesley SA]] | ||
[[Category: | [[Category: Mathews II]] | ||
Revision as of 10:17, 26 October 2022
T. Maritima FDTS (R174K mutant) with FADT. Maritima FDTS (R174K mutant) with FAD
Structural highlights
FunctionTHYX_THEMA Catalyzes the formation of dTMP and tetrahydrofolate from dUMP and methylenetetrahydrofolate. Publication Abstract from PubMedThe DNA nucleotide thymidylate is synthesized by the enzyme thymidylate synthase, which catalyzes the reductive methylation of deoxyuridylate using the cofactor methylene-tetrahydrofolate (CH(2)H(4)folate). Most organisms, including humans, rely on the thyA- or TYMS-encoded classic thymidylate synthase, whereas, certain microorganisms, including all Rickettsia and other pathogens, use an alternative thyX-encoded flavin-dependent thymidylate synthase (FDTS). Although several crystal structures of FDTSs have been reported, the absence of a structure with folates limits understanding of the molecular mechanism and the scope of drug design for these enzymes. Here we present X-ray crystal structures of FDTS with several folate derivatives, which together with mutagenesis, kinetic analysis, and computer modeling shed light on the cofactor binding and function. The unique structural data will likely facilitate further elucidation of FDTSs' mechanism and the design of structure-based inhibitors as potential leads to new antimicrobial drugs. Folate binding site of flavin-dependent thymidylate synthase.,Koehn EM, Perissinotti LL, Moghram S, Prabhakar A, Lesley SA, Mathews II, Kohen A Proc Natl Acad Sci U S A. 2012 Sep 25;109(39):15722-7. Epub 2012 Sep 10. PMID:23019356[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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