4wxg: Difference between revisions
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==Crystal structure of L-Serine Hydroxymethyltransferase in complex with a mixture of L | ==Crystal structure of L-Serine Hydroxymethyltransferase in complex with a mixture of L-Threonine and Glycine== | ||
<StructureSection load='4wxg' size='340' side='right' caption='[[4wxg]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='4wxg' size='340' side='right'caption='[[4wxg]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4wxg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WXG OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4wxg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_thermophilus_CNRZ1066 Streptococcus thermophilus CNRZ1066]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WXG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WXG FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2BO:N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-L-THREONINE'>2BO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2BO:N-({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)-L-THREONINE'>2BO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wxg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wxg OCA], [https://pdbe.org/4wxg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wxg RCSB], [https://www.ebi.ac.uk/pdbsum/4wxg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wxg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/GLYA_STRT1 GLYA_STRT1] Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 21: | Line 21: | ||
==See Also== | ==See Also== | ||
*[[Serine hydroxymethyltransferase|Serine hydroxymethyltransferase]] | *[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bujons | [[Category: Streptococcus thermophilus CNRZ1066]] | ||
[[Category: Clapes | [[Category: Bujons J]] | ||
[[Category: Hernandez | [[Category: Clapes P]] | ||
[[Category: Joglar | [[Category: Hernandez K]] | ||
[[Category: Parella | [[Category: Joglar J]] | ||
[[Category: Petrillo | [[Category: Parella T]] | ||
[[Category: Uson | [[Category: Petrillo G]] | ||
[[Category: Wandtke | [[Category: Uson I]] | ||
[[Category: Zelen | [[Category: Wandtke C]] | ||
[[Category: Zelen I]] | |||
Latest revision as of 13:45, 10 January 2024
Crystal structure of L-Serine Hydroxymethyltransferase in complex with a mixture of L-Threonine and GlycineCrystal structure of L-Serine Hydroxymethyltransferase in complex with a mixture of L-Threonine and Glycine
Structural highlights
FunctionGLYA_STRT1 Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Publication Abstract from PubMedalpha,alpha-Disubstituted alpha-amino acids are central to biotechnological and biomedical chemical processes for their own sake and as substructures of biologically active molecules for diverse biomedical applications. Structurally, these compounds contain a quaternary stereocenter, which is particularly challenging for stereoselective synthesis. The pyridoxal-5'-phosphate (PLP)-dependent L-serine hydroxymethyltransferase from Streptococcus thermophilus (SHMTSth ; EC 2.1.2.1) was engineered to achieve the stereoselective synthesis of a broad structural variety of alpha,alpha-dialkyl-alpha-amino acids. This was accomplished by the formation of quaternary stereocenters through aldol addition of the amino acids D-Ala and D-Ser to a wide acceptor scope catalyzed by the minimalist SHMTSth Y55T variant overcoming the limitation of the native enzyme for Gly. The SHMTSth Y55T variant tolerates aromatic and aliphatic aldehydes as well as hydroxy- and nitrogen-containing aldehydes as acceptors. Engineered L-Serine Hydroxymethyltransferase from Streptococcus thermophilus for the Synthesis of alpha,alpha-Dialkyl-alpha-Amino Acids.,Hernandez K, Zelen I, Petrillo G, Uson I, Wandtke CM, Bujons J, Joglar J, Parella T, Clapes P Angew Chem Int Ed Engl. 2015 Jan 21. doi: 10.1002/anie.201411484. PMID:25611820[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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