6eac

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Current revision (14:40, 13 March 2024) (edit) (undo)
 
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<StructureSection load='6eac' size='340' side='right'caption='[[6eac]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
<StructureSection load='6eac' size='340' side='right'caption='[[6eac]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6eac]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_19310 Atcc 19310]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EAC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EAC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6eac]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_syringae Pseudomonas syringae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EAC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 2.269&#8491;</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=6eac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eac OCA], [http://pdbe.org/6eac PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eac RCSB], [http://www.ebi.ac.uk/pdbsum/6eac PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eac ProSAT]</span></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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6eac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eac OCA], [https://pdbe.org/6eac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6eac RCSB], [https://www.ebi.ac.uk/pdbsum/6eac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6eac ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/SELO_PSESM SELO_PSESM] Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).[HAMAP-Rule:MF_00692]<ref>PMID:30270044</ref>
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Approximately 10% of human protein kinases are believed to be inactive and named pseudokinases because they lack residues required for catalysis. Here, we show that the highly conserved pseudokinase selenoprotein-O (SelO) transfers AMP from ATP to Ser, Thr, and Tyr residues on protein substrates (AMPylation), uncovering a previously unrecognized activity for a member of the protein kinase superfamily. The crystal structure of a SelO homolog reveals a protein kinase-like fold with ATP flipped in the active site, thus providing a structural basis for catalysis. SelO pseudokinases localize to the mitochondria and AMPylate proteins involved in redox homeostasis. Consequently, SelO activity is necessary for the proper cellular response to oxidative stress. Our results suggest that AMPylation may be a more widespread post-translational modification than previously appreciated and that pseudokinases should be analyzed for alternative transferase activities.
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Protein AMPylation by an Evolutionarily Conserved Pseudokinase.,Sreelatha A, Yee SS, Lopez VA, Park BC, Kinch LN, Pilch S, Servage KA, Zhang J, Jiou J, Karasiewicz-Urbanska M, Lobocka M, Grishin NV, Orth K, Kucharczyk R, Pawlowski K, Tomchick DR, Tagliabracci VS Cell. 2018 Sep 25. pii: S0092-8674(18)31107-3. doi: 10.1016/j.cell.2018.08.046. PMID:30270044<ref>PMID:30270044</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6eac" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 19310]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Sreelatha, A]]
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[[Category: Pseudomonas syringae]]
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[[Category: Tagliabracci, V S]]
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[[Category: Sreelatha A]]
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[[Category: Tomchick, D R]]
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[[Category: Tagliabracci VS]]
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[[Category: Adenylylation]]
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[[Category: Tomchick DR]]
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[[Category: Ampylation]]
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[[Category: Atypical kinase fold]]
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[[Category: Flipped atp]]
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[[Category: Oxidative stress]]
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[[Category: Pseudokinase]]
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[[Category: Selenocysteine]]
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[[Category: Selenoprotein]]
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[[Category: Transferase]]
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Current revision

Pseudomonas syringae SelO

PDB ID 6eac

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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