4bhd: Difference between revisions
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==Methanococcus jannaschii serine hydroxymethyl-transferase, apo form== | |||
<StructureSection load='4bhd' size='340' side='right' caption='[[4bhd]], [[Resolution|resolution]] 2.83Å' scene=''> | |||
== Structural highlights == | |||
==Function== | <table><tr><td colspan='2'>[[4bhd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BHD FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bhe|4bhe]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4bhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bhd RCSB], [http://www.ebi.ac.uk/pdbsum/4bhd PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref> | [[http://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref> | ||
== | ==See Also== | ||
[[ | *[[Serine hydroxymethyltransferase|Serine hydroxymethyltransferase]] | ||
== References == | |||
== | <references/> | ||
<references | __TOC__ | ||
[[Category: Angelucci, F | </StructureSection> | ||
[[Category: Ilari, A | [[Category: Atcc 43067]] | ||
[[Category: Saccoccia, F | [[Category: Angelucci, F]] | ||
[[Category: Ilari, A]] | |||
[[Category: Saccoccia, F]] | |||
[[Category: Transferase]] | [[Category: Transferase]] | ||
