5lrt

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m (Protected "5lrt" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5lrt is ON HOLD until Paper Publication
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==Structure of the Deamidase-Depupylase Dop of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ADP and Phosphate==
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<StructureSection load='5lrt' size='340' side='right' caption='[[5lrt]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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Authors:
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5lrt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LRT FirstGlance]. <br>
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Description:
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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[[Category: Unreleased Structures]]
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4b0s|4b0s]], [[4b0r|4b0r]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5lrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lrt OCA], [http://pdbe.org/5lrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lrt RCSB], [http://www.ebi.ac.uk/pdbsum/5lrt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lrt ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://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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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Ban, N]]
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[[Category: Bolten, M]]
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[[Category: Leibundgut, M]]
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[[Category: Lipp, C]]
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[[Category: Vahlensieck, C]]
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[[Category: Weber-Ban, E]]
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[[Category: Complex]]
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[[Category: Hydrolase]]

Revision as of 18:07, 1 February 2017

Structure of the Deamidase-Depupylase Dop of the Prokaryotic Ubiquitin-like Modification Pathway in Complex with ADP and Phosphate

5lrt, resolution 1.85Å

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