3p1b: Difference between revisions

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 <StructureSection load='3p1b' size='340' side='right'caption='[[3p1b]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3p1b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica_hm-1:imss Entamoeba histolytica hm-1:imss]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P1B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3p1b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica_HM-1:IMSS Entamoeba histolytica HM-1:IMSS]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P1B FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.77&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1t3d|1t3d]], [[1ssm|1ssm]], [[1sst|1sst]], [[1ssq|1ssq]], [[3p47|3p47]], [[3q1x|3q1x]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CysE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=294381 Entamoeba histolytica HM-1:IMSS])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Serine_O-acetyltransferase Serine O-acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.30 2.3.1.30] </span></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=3p1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p1b OCA], [https://pdbe.org/3p1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p1b RCSB], [https://www.ebi.ac.uk/pdbsum/3p1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p1b ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[https://www.uniprot.org/uniprot/Q9U8X2_ENTHI Q9U8X2_ENTHI]
-Cysteine (cys) plays a major role in growth and survival of the human parasite Entamoeba histolytica. We report here the crystal structure of serine acetyltransferase (SAT) isoform1, a cysteine biosynthetic pathway enzyme, from E. histolytica (EhSAT1) at 1.77 [Aring], in complex with its substrate serine (ser) at 1.59 [Aring] and inhibitor cys at 1.78 [Aring] resolution. EhSAT1 exists as a trimer both in solution as well as in crystal structure, unlike hexamers formed by other known SATs. The difference in oligomeric state is due to the N- terminal region of the EhSAT1, which has very low sequence similarity to known structures, also differs in orientation and charge distribution. The ser and cys bind to the same site, confirming that cys is a competitive inhibitor of ser. The disordered C-terminal region and the loop near the active site are responsible for solvent accessible acetyl Co-A binding site and thus lose inhibition to acetyl Co-A by the feedback inhibitor cys. Docking and fluorescence studies show that EhSAT1 C-terminal mimicking peptides can bind to o-acetyl serine sulfhydrylase (EhOASS), while native C-terminal peptide does not show any binding. To test further, C-terminal end of EhSAT1 was mutated and found that it inhibits EhOASS, confirming modified EhSAT1 can bind to EhOASS. The apparent inability of EhSAT1 to form a hexamer and differences in C-terminal region are likely to be the major reasons for the lack of formation of the large cysteine synthase complex and loss of a complex regulatory mechanism in E. histolytica.
-Structural and biochemical studies of serine acetyltransferase reveal why the parasite Entamoeba histolytica cannot form cysteine synthase complex.,Kumar S, Raj I, Nagpal I, Subbarao N, Gourinath S J Biol Chem. 2011 Feb 5. PMID:21297164<ref>PMID:21297164</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3p1b" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Serine acetyltransferase|Serine acetyltransferase]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Entamoeba histolytica hm-1:imss]]
+[[Category: Entamoeba histolytica HM-1:IMSS]]
 [[Category: Large Structures]]
-[[Category: Serine O-acetyltransferase]]
+[[Category: Gourinath S]]
-[[Category: Gourinath, S]]
+[[Category: Kumar S]]
-[[Category: Kumar, S]]
-[[Category: Cysteine synthesis]]
-[[Category: Serine acetyltransferase]]
-[[Category: Transferase]]