4bwf: Difference between revisions
New page: '''Unreleased structure''' The entry 4bwf is ON HOLD Authors: Williams, C., van den Berg, M., Stanley, W.A., Wilmanns, M., Distel, B. Description: Pex4p-Pex22p disulphide bond mutant |
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==Pex4p-Pex22p disulphide bond mutant== | |||
<StructureSection load='4bwf' size='340' side='right'caption='[[4bwf]], [[Resolution|resolution]] 3.23Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4bwf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2y9o 2y9o]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BWF 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]] 3.23Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=4bwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bwf OCA], [https://pdbe.org/4bwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bwf RCSB], [https://www.ebi.ac.uk/pdbsum/4bwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bwf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/UBCX_YEAST UBCX_YEAST] Catalyzes the covalent attachment of ubiquitin to other proteins. Essential for peroxisome biogenesis. Required for UBC4-independent ubiquitination of PEX5. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ubiquitin-conjugating enzyme Pex4p together with its binding partner, the peroxisomal membrane protein Pex22p, co-ordinates cysteine-dependent ubiquitination of the cycling receptor protein Pex5p. Unusually for an ubiquitin-conjugating enzyme, Saccharomyces cerevisiae Pex4p can form a disulphide bond between the cysteine residues at positions 105 and 146. We found that mutating the disulphide forming cysteine residues in Pex4p to serines does not disturb the secondary structure of the protein but does reduce the in vitro activity of Pex4p. From the crystal structure of Pex4p C105S, C146S in complex with the soluble domain of Pex22p, we observe a narrowing of the active site cleft, caused by loss of the disulphide bond. This modification of the active site microenvironment is likely to restrict access of ubiquitin to the active site cysteine, modulating Pex4p activity. Finally, based on sequence and structural alignments, we have identified other ubiquitin-conjugating enzymes that may contain disulphide bonds. | |||
A disulphide bond in the E2 enzyme Pex4p modulates ubiquitin-conjugating activity.,Williams C, van den Berg M, Stanley WA, Wilmanns M, Distel B Sci Rep. 2013 Jul 30;3:2212. doi: 10.1038/srep02212. PMID:23896733<ref>PMID:23896733</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4bwf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | |||
[[Category: Distel B]] | |||
[[Category: Stanley WA]] | |||
[[Category: Williams C]] | |||
[[Category: Wilmanns M]] | |||
[[Category: Van den Berg M]] | |||
Latest revision as of 14:59, 20 December 2023
Pex4p-Pex22p disulphide bond mutantPex4p-Pex22p disulphide bond mutant
Structural highlights
FunctionUBCX_YEAST Catalyzes the covalent attachment of ubiquitin to other proteins. Essential for peroxisome biogenesis. Required for UBC4-independent ubiquitination of PEX5. Publication Abstract from PubMedThe ubiquitin-conjugating enzyme Pex4p together with its binding partner, the peroxisomal membrane protein Pex22p, co-ordinates cysteine-dependent ubiquitination of the cycling receptor protein Pex5p. Unusually for an ubiquitin-conjugating enzyme, Saccharomyces cerevisiae Pex4p can form a disulphide bond between the cysteine residues at positions 105 and 146. We found that mutating the disulphide forming cysteine residues in Pex4p to serines does not disturb the secondary structure of the protein but does reduce the in vitro activity of Pex4p. From the crystal structure of Pex4p C105S, C146S in complex with the soluble domain of Pex22p, we observe a narrowing of the active site cleft, caused by loss of the disulphide bond. This modification of the active site microenvironment is likely to restrict access of ubiquitin to the active site cysteine, modulating Pex4p activity. Finally, based on sequence and structural alignments, we have identified other ubiquitin-conjugating enzymes that may contain disulphide bonds. A disulphide bond in the E2 enzyme Pex4p modulates ubiquitin-conjugating activity.,Williams C, van den Berg M, Stanley WA, Wilmanns M, Distel B Sci Rep. 2013 Jul 30;3:2212. doi: 10.1038/srep02212. PMID:23896733[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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