4zdo: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4zdo]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZDO FirstGlance]. <br> | <table><tr><td colspan='2'>[[4zdo]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZDO FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLR:(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL+DIHYDROGEN+PHOSPHATE'>PLR</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.65Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLR:(5-HYDROXY-4,6-DIMETHYLPYRIDIN-3-YL)METHYL+DIHYDROGEN+PHOSPHATE'>PLR</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=4zdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdo OCA], [https://pdbe.org/4zdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zdo RCSB], [https://www.ebi.ac.uk/pdbsum/4zdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zdo ProSAT]</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=4zdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zdo OCA], [https://pdbe.org/4zdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zdo RCSB], [https://www.ebi.ac.uk/pdbsum/4zdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zdo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 11:16, 27 September 2023
The crystal structure of T325S mutant of human SepSecS in complex with selenocysteine tRNA (tRNASec)The crystal structure of T325S mutant of human SepSecS in complex with selenocysteine tRNA (tRNASec)
Structural highlights
FunctionPublication Abstract from PubMedSelenocysteine synthase (SepSecS) catalyzes the terminal reaction of selenocysteine, and is vital for human selenoproteome integrity. Autosomal recessive inheritance of mutations in SepSecS-Ala239Thr, Thr325Ser, Tyr334Cys and Tyr429*-induced severe, early-onset, neurological disorders in distinct human populations. Although harboring different mutant alleles, patients presented remarkably similar phenotypes typified by cerebellar and cerebral atrophy, seizures, irritability, ataxia, and extreme spasticity. However, it has remained unclear how these genetic alterations affected the structure of SepSecS and subsequently elicited the development of a neurological pathology. Herein, our biophysical and structural characterization demonstrates that, with the exception of Tyr429*, pathogenic mutations decrease protein stability and trigger protein misfolding. We propose that the reduced stability and increased propensity towards misfolding are the main causes for the loss of SepSecS activity in afflicted patients, and that these factors contribute to disease progression. We also suggest that misfolding of enzymes regulating protein synthesis should be considered in the diagnosis and study of childhood neurological disorders. Structural basis for early-onset neurological disorders caused by mutations in human selenocysteine synthase.,Puppala AK, French RL, Matthies D, Baxa U, Subramaniam S, Simonovic M Sci Rep. 2016 Aug 31;6:32563. doi: 10.1038/srep32563. PMID:27576344[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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