4h6d: Difference between revisions
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==Crystal structure of PLP-soaked HMP synthase Thi5 from S. cerevisiae== | ==Crystal structure of PLP-soaked HMP synthase Thi5 from S. cerevisiae== | ||
<StructureSection load='4h6d' size='340' side='right' caption='[[4h6d]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='4h6d' size='340' side='right'caption='[[4h6d]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4h6d]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4h6d]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H6D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H6D FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=4h6d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h6d OCA], [https://pdbe.org/4h6d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h6d RCSB], [https://www.ebi.ac.uk/pdbsum/4h6d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h6d 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/THI5_YEAST THI5_YEAST] Proposed biosynthetic enzyme involved in pyrimidine biosynthesis pathway above the hydroxymethyl-pyrimidine precursor leading to the thiamine moiety.<ref>PMID:12777485</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 22: | Line 20: | ||
==See Also== | ==See Also== | ||
*[[Endonuclease|Endonuclease]] | *[[Endonuclease 3D structures|Endonuclease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Coquille | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Fitzpatrick | [[Category: Coquille SC]] | ||
[[Category: Roux | [[Category: Fitzpatrick T]] | ||
[[Category: Thore | [[Category: Roux C]] | ||
[[Category: Thore S]] | |||
Revision as of 11:02, 3 November 2022
Crystal structure of PLP-soaked HMP synthase Thi5 from S. cerevisiaeCrystal structure of PLP-soaked HMP synthase Thi5 from S. cerevisiae
Structural highlights
FunctionTHI5_YEAST Proposed biosynthetic enzyme involved in pyrimidine biosynthesis pathway above the hydroxymethyl-pyrimidine precursor leading to the thiamine moiety.[1] Publication Abstract from PubMedVitamin B1 is essential for all organisms being well recognized as a necessary cofactor for key metabolic pathways such as glycolysis and was more recently implicated in DNA damage responses. Little is known about the enzyme responsible for the formation of the pyrimidine moiety (HMP-P synthase). We report a structure-function study of the HMP-P synthase from yeast, THI5p. Our crystallographic structure shows that the THI5p is a mix between periplasmic binding proteins and pyridoxal 5'-phosphate (PLP) dependent enzymes. Mutational and yeast complementation studies identify the key residues for HMP-P biosynthesis and offers unprecedented insights into the use of PLP as a substrate rather than as a cofactor, the requirement of iron and more generally into the HMP-P synthase reaction mechanism. The last piece in the vitamin B1 biosynthesis puzzle: Structural and functional insight into yeast HMP-P synthase.,Coquille S, Roux C, Fitzpatrick TB, Thore S J Biol Chem. 2012 Oct 9. PMID:23048037[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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