5yd2: Difference between revisions
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<StructureSection load='5yd2' size='340' side='right'caption='[[5yd2]], [[Resolution|resolution]] 2.35Å' scene=''> | <StructureSection load='5yd2' size='340' side='right'caption='[[5yd2]], [[Resolution|resolution]] 2.35Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5yd2]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5yd2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica_HM-3:IMSS Entamoeba histolytica HM-3:IMSS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YD2 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]] 2.35Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5yd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yd2 OCA], [https://pdbe.org/5yd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yd2 RCSB], [https://www.ebi.ac.uk/pdbsum/5yd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yd2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/M7XC02_ENTHI M7XC02_ENTHI] | |||
<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 5yd2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5yd2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Phosphoserine aminotransferase|Phosphoserine aminotransferase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Entamoeba histolytica | [[Category: Entamoeba histolytica HM-3:IMSS]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Gourinath | [[Category: Gourinath S]] | ||
[[Category: Singh | [[Category: Singh RK]] | ||
Latest revision as of 11:27, 22 November 2023
Crystal Structure of Delta 4 mutant of EhPSAT (Phosphoserine aminotransferase of Entamoeba histolytica)Crystal Structure of Delta 4 mutant of EhPSAT (Phosphoserine aminotransferase of Entamoeba histolytica)
Structural highlights
FunctionPublication Abstract from PubMedPhosphoserine aminotransferase (PSAT) is a pyridoxal-5'phosphate (PLP)-dependent enzyme that catalyzes the second reversible step in the phosphoserine biosynthetic pathway producing serine. The crystal structure of E. histolytica PSAT (EhPSAT) complexed with PLP was elucidated at 3.0A resolution and the structures of its mutants, EhPSAT_Delta45 and EhPSAT_Delta4, at 1.8 and 2.4A resolution respectively. Deletion of 45 N-terminal residues (EhPSAT_Delta45) resulted in an inactive protein, the structure showed a dimeric arrangement drastically different from that of the wild-type protein, with the two monomers translated and rotated by almost 180 degrees with respect to each other; causing a rearrangement of the active site to which PLP was unable to bind. Deletion of first N-terminal 15 (EhPSAT_Delta15) and four 11th to 14th residues (EhPSAT_Delta4) yielded up to 98% and 90% decrease in the activity respectively. Absence of aldimine linkage between PLP-Lys in the crystal structure of EhPSAT_Delta4 mutant explains for such decrease in activity and describes the importance of these N-terminal residues. Furthermore, a halide-binding site was found in close proximity to the active site. A stretch of six amino acids (146-NNTIYG-151) only conserved in the Entamoeba genus, contributes to halide binding may explain that the halide inhibition could be specific to Entamoeba. N-terminal residues are crucial for quaternary structure and active site conformation for the phosphoserine aminotransferase from enteric human parasite E. histolytica.,Singh RK, Tomar P, Dharavath S, Kumar S, Gourinath S Int J Biol Macromol. 2019 Jul 1;132:1012-1023. doi:, 10.1016/j.ijbiomac.2019.04.027. Epub 2019 Apr 5. PMID:30959130[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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