1hjz
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='1hjz' size='340' side='right'caption='[[1hjz]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='1hjz' size='340' side='right'caption='[[1hjz]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1hjz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1hjz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HJZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HJZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></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]] 1.7Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</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=1hjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hjz OCA], [https://pdbe.org/1hjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hjz RCSB], [https://www.ebi.ac.uk/pdbsum/1hjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hjz 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=1hjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hjz OCA], [https://pdbe.org/1hjz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hjz RCSB], [https://www.ebi.ac.uk/pdbsum/1hjz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hjz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/Y1521_ARCFU Y1521_ARCFU] Removes ADP-ribose from glutamate residues in proteins bearing a single ADP-ribose moiety. Inactive towards proteins bearing poly-ADP-ribose. Catalyzes removal of a phosphate group from ADP-ribose 1''-phosphate (Appr1p), but with low efficiency.<ref>PMID:23474712</ref> <ref>PMID:15902274</ref> | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 19: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hjz ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hjz ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | MacroH2A is an unusual histone H2A variant that has an extensive C-terminal tail that comprises approximately two thirds of the protein. The C-terminal non-histone domain of macroH2A is also found in a number of other proteins and has been termed the macro domain. Here we report the crystal structure to 1.7A of AF1521, a protein consisting of a stand-alone macro domain from Archaeoglobus fulgidus. The structure has a mixed alpha/beta fold that closely resembles the N-terminal DNA binding domain of the Escherichia coli leucine aminopeptidase PepA. The structure also shows some similarity to members of the P-loop family of nucleotide hydrolases. | ||
| - | |||
| - | The crystal structure of AF1521 a protein from Archaeoglobus fulgidus with homology to the non-histone domain of macroH2A.,Allen MD, Buckle AM, Cordell SC, Lowe J, Bycroft M J Mol Biol. 2003 Jul 11;330(3):503-11. PMID:12842467<ref>PMID:12842467</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1hjz" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Archaeoglobus fulgidus]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Allen | + | [[Category: Allen MD]] |
| - | [[Category: Buckle | + | [[Category: Buckle AM]] |
| - | [[Category: Bycroft | + | [[Category: Bycroft M]] |
| - | [[Category: Cordell | + | [[Category: Cordell SC]] |
| - | [[Category: Lowe | + | [[Category: Lowe J]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Revision as of 11:32, 27 March 2024
Crystal structure of AF1521 protein containing a macroH2A domain
| |||||||||||
