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==X-ray crystal structure of a serine hydroxymethyl transferase in apo form from Burkholderia cenocepacia== | ==X-ray crystal structure of a serine hydroxymethyl transferase in apo form from Burkholderia cenocepacia== | ||
<StructureSection load='4mso' size='340' side='right' caption='[[4mso]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='4mso' size='340' side='right'caption='[[4mso]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4mso]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4mso]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_cenocepacia_J2315 Burkholderia cenocepacia J2315]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MSO FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4Å</td></tr> | ||
<tr id=' | <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=PO4:PHOSPHATE+ION'>PO4</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=4mso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mso OCA], [https://pdbe.org/4mso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mso RCSB], [https://www.ebi.ac.uk/pdbsum/4mso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mso 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/B4ECY9_BURCJ B4ECY9_BURCJ] 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 (By similarity).[HAMAP-Rule:MF_00051] | ||
==See Also== | ==See Also== | ||
*[[Serine hydroxymethyltransferase|Serine hydroxymethyltransferase]] | *[[Serine hydroxymethyltransferase 3D structures|Serine hydroxymethyltransferase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Burkholderia cenocepacia J2315]] | ||
[[Category: | [[Category: Large Structures]] | ||
Latest revision as of 19:41, 20 September 2023
X-ray crystal structure of a serine hydroxymethyl transferase in apo form from Burkholderia cenocepaciaX-ray crystal structure of a serine hydroxymethyl transferase in apo form from Burkholderia cenocepacia
Structural highlights
FunctionB4ECY9_BURCJ 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 (By similarity).[HAMAP-Rule:MF_00051] See Also |
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