7oyh
From Proteopedia
(Difference between revisions)
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| - | ==== | + | ==Crystal structure of depupylase Dop in complex with Pup and ADP/tetrafluoromagnesate== |
| - | <StructureSection load='7oyh' size='340' side='right'caption='[[7oyh]]' scene=''> | + | <StructureSection load='7oyh' size='340' side='right'caption='[[7oyh]], [[Resolution|resolution]] 1.75Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7oyh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidothermus_cellulolyticus Acidothermus cellulolyticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OYH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OYH FirstGlance]. <br> |
| - | </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=7oyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oyh OCA], [https://pdbe.org/7oyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oyh RCSB], [https://www.ebi.ac.uk/pdbsum/7oyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oyh ProSAT]</span></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]] 1.75Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MF4:TETRAFLUOROMAGNESATE(2-)'>MF4</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7oyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oyh OCA], [https://pdbe.org/7oyh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oyh RCSB], [https://www.ebi.ac.uk/pdbsum/7oyh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oyh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PUP_ACIC1 PUP_ACIC1] Protein modifier that is covalently attached to lysine residues of substrate proteins, thereby targeting them for proteasomal degradation. The tagging system is termed pupylation.[HAMAP-Rule:MF_02106] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pupylation is the post-translational modification of lysine side chains with prokaryotic ubiquitin-like protein (Pup) that targets proteins for proteasomal degradation in mycobacteria and other members of Actinobacteria. Pup ligase PafA and depupylase Dop are the two enzymes acting in this pathway. Although they share close structural and sequence homology indicative of a common evolutionary origin, they catalyze opposing reactions. Here, we report a series of high-resolution crystal structures of Dop in different functional states along the reaction pathway, including Pup-bound states in distinct conformations. In combination with biochemical analysis, the structures explain the role of the C-terminal residue of Pup in ATP hydrolysis, the process that generates the catalytic phosphate in the active site, and suggest a role for the Dop-loop as an allosteric sensor for Pup-binding and ATP cleavage. | ||
| + | |||
| + | Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation.,Cui H, Muller AU, Leibundgut M, Tian J, Ban N, Weber-Ban E Nat Commun. 2021 Nov 17;12(1):6635. doi: 10.1038/s41467-021-26848-x. PMID:34789727<ref>PMID:34789727</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7oyh" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Acidothermus cellulolyticus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Cui H]] |
Current revision
Crystal structure of depupylase Dop in complex with Pup and ADP/tetrafluoromagnesate
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