4b0s

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Current revision (10:55, 9 May 2024) (edit) (undo)
 
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<StructureSection load='4b0s' size='340' side='right'caption='[[4b0s]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
<StructureSection load='4b0s' size='340' side='right'caption='[[4b0s]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4b0s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acic1 Acic1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B0S FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4b0s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acidothermus_cellulolyticus_11B Acidothermus cellulolyticus 11B]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4B0S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4B0S FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4b0r|4b0r]], [[4b0t|4b0t]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4b0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b0s OCA], [https://pdbe.org/4b0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b0s RCSB], [https://www.ebi.ac.uk/pdbsum/4b0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b0s 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=4b0s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4b0s OCA], [https://pdbe.org/4b0s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4b0s RCSB], [https://www.ebi.ac.uk/pdbsum/4b0s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4b0s ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/DOP_ACIC1 DOP_ACIC1]] Displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Is also able to catalyze the deamidation of the C-terminal glutamine to glutamate in a variant of the prokaryotic ubiquitin-like protein Pup; however, since Pup from A.cellulolyticus possesses a C-terminal glutamate, this deamidase activity may be of no significance in vivo.<ref>PMID:22910360</ref>
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[https://www.uniprot.org/uniprot/DOP_ACIC1 DOP_ACIC1] Displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; is thus involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins. Is also able to catalyze the deamidation of the C-terminal glutamine to glutamate in a variant of the prokaryotic ubiquitin-like protein Pup; however, since Pup from A.cellulolyticus possesses a C-terminal glutamate, this deamidase activity may be of no significance in vivo.<ref>PMID:22910360</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acic1]]
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[[Category: Acidothermus cellulolyticus 11B]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Allain, F H.T]]
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[[Category: Allain FH-T]]
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[[Category: Ban, N]]
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[[Category: Ban N]]
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[[Category: Barandun, J]]
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[[Category: Barandun J]]
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[[Category: Damberger, F F]]
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[[Category: Damberger FF]]
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[[Category: Guth, E]]
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[[Category: Guth E]]
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[[Category: Ozcelik, D]]
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[[Category: Ozcelik D]]
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[[Category: Schmitz, N]]
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[[Category: Schmitz N]]
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[[Category: Sutter, M]]
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[[Category: Sutter M]]
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[[Category: Weber-Ban, E]]
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[[Category: Weber-Ban E]]
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[[Category: Hydrolase]]
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[[Category: Prokaryotic ubiquitin-like protein]]
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[[Category: Proteasome]]
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[[Category: Pupylation]]
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Current revision

Structure of the Deamidase-Depupylase Dop of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ATP

PDB ID 4b0s

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OCA

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