8gn9: Difference between revisions
New page: '''Unreleased structure''' The entry 8gn9 is ON HOLD Authors: Komatsu, T., Matsui, I., Yokoyama, H. Description: SPFH domain of Pyrococcus horikoshii stomatin [[Category: Unreleased St... |
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==SPFH domain of Pyrococcus horikoshii stomatin== | |||
<StructureSection load='8gn9' size='340' side='right'caption='[[8gn9]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8gn9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8GN9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8GN9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=8gn9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8gn9 OCA], [https://pdbe.org/8gn9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8gn9 RCSB], [https://www.ebi.ac.uk/pdbsum/8gn9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8gn9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PSTOM_PYRHO PSTOM_PYRHO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Stomatin is a major integral membrane protein in human erythrocytes. In a form of hemolytic anemia known as hereditary stomatocytosis, stomatin is deficient in the erythrocyte membrane due to mis-trafficking. It is a member of stomatin, prohibitin, flotillin, and HflK/C (SPFH) domain proteins, and SPFH proteins could function as membrane-bound oligomeric scaffolding proteins in lipid rafts. The previously determined structure of the SPFH domain of Pyrococcus horikoshii (Ph) stomatin formed a trimer, whereas that of mouse stomatin formed a dimer. To elucidate the difference of oligomerization state, structural and chromatographic analyses using Ph stomatin were performed, and the key residues were suggested to determine whether SPFH domains form dimers or trimers. From gel-filtration analyses, PhStom (56-234) formed a trimer or tetramer, whereas PhStom (63-234) and PhStom (56-234) K59S formed a dimer. The residues 56-62, particularly Lys59, were involved in trimerization. Based on the crystal structure of PhStom (63-234), it formed a banana-shaped dimer, as observed in mouse stomatin. Thus, residues 162-168 are involved in dimerization. This study provides important insight into the molecular function and oligomerization state of stomatin. | |||
Structural and mutational studies suggest key residues to determine whether stomatin SPFH domains form dimers or trimers.,Komatsu T, Matsui I, Yokoyama H Biochem Biophys Rep. 2022 Nov 11;32:101384. doi: 10.1016/j.bbrep.2022.101384. , eCollection 2022 Dec. PMID:36386441<ref>PMID:36386441</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8gn9" style="background-color:#fffaf0;"></div> | ||
[[Category: Komatsu | == References == | ||
[[Category: Matsui | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pyrococcus horikoshii]] | |||
[[Category: Komatsu T]] | |||
[[Category: Matsui I]] | |||
[[Category: Yokoyama H]] | |||
Latest revision as of 21:12, 29 November 2023
SPFH domain of Pyrococcus horikoshii stomatinSPFH domain of Pyrococcus horikoshii stomatin
Structural highlights
FunctionPublication Abstract from PubMedStomatin is a major integral membrane protein in human erythrocytes. In a form of hemolytic anemia known as hereditary stomatocytosis, stomatin is deficient in the erythrocyte membrane due to mis-trafficking. It is a member of stomatin, prohibitin, flotillin, and HflK/C (SPFH) domain proteins, and SPFH proteins could function as membrane-bound oligomeric scaffolding proteins in lipid rafts. The previously determined structure of the SPFH domain of Pyrococcus horikoshii (Ph) stomatin formed a trimer, whereas that of mouse stomatin formed a dimer. To elucidate the difference of oligomerization state, structural and chromatographic analyses using Ph stomatin were performed, and the key residues were suggested to determine whether SPFH domains form dimers or trimers. From gel-filtration analyses, PhStom (56-234) formed a trimer or tetramer, whereas PhStom (63-234) and PhStom (56-234) K59S formed a dimer. The residues 56-62, particularly Lys59, were involved in trimerization. Based on the crystal structure of PhStom (63-234), it formed a banana-shaped dimer, as observed in mouse stomatin. Thus, residues 162-168 are involved in dimerization. This study provides important insight into the molecular function and oligomerization state of stomatin. Structural and mutational studies suggest key residues to determine whether stomatin SPFH domains form dimers or trimers.,Komatsu T, Matsui I, Yokoyama H Biochem Biophys Rep. 2022 Nov 11;32:101384. doi: 10.1016/j.bbrep.2022.101384. , eCollection 2022 Dec. PMID:36386441[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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