1dm5
From Proteopedia
(Difference between revisions)
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<StructureSection load='1dm5' size='340' side='right'caption='[[1dm5]], [[Resolution|resolution]] 1.93Å' scene=''> | <StructureSection load='1dm5' size='340' side='right'caption='[[1dm5]], [[Resolution|resolution]] 1.93Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1dm5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1dm5]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Hydra_vulgaris Hydra vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DM5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DM5 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1dm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dm5 OCA], [https://pdbe.org/1dm5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dm5 RCSB], [https://www.ebi.ac.uk/pdbsum/1dm5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dm5 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=1dm5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dm5 OCA], [https://pdbe.org/1dm5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dm5 RCSB], [https://www.ebi.ac.uk/pdbsum/1dm5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dm5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ANX12_HYDVU ANX12_HYDVU] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</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=1dm5 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=1dm5 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Annexins are a family of calcium- and phospholipid-binding proteins involved with numerous cellular processes including membrane fusion, ion channel activity, and heterocomplex formation with other proteins. The annexin XII (ANXB12) crystal structure presented evidence that calcium mediates the formation of a hexamer through a novel intermolecular calcium-binding site [Luecke et al. (1995) Nature 378, 512-515]. In an attempt to disrupt hexamerization, we mutated a conserved key ligand in the intermolecular calcium-binding site, Glu105, to lysine. Despite its occurrence in a new spacegroup, the 1.93 A resolution structure reveals a hexamer with the Lys105 epsilon-amino group nearly superimposable with the original intermolecular calcium position. Our analysis shows that the mutation is directly involved in stabilizing the hexamer. The local residues are reoriented to retain affinity between the two trimers via a pH-dependent switch residue, Glu76, which is now protonated, allowing it to form tandem hydrogen bonds with the backbone carbonyl and nitrogen atoms of Thr103 located across the trimer interface. The loss of the intermolecular calcium-binding site is recuperated by extensive hydrogen bonding favoring hexamer stabilization. The presence of this mutant structure provides further evidence for hexameric annexin XII, and possible in vivo roles are discussed. | ||
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| - | Annexin XII E105K crystal structure: identification of a pH-dependent switch for mutant hexamerization.,Cartailler JP, Haigler HT, Luecke H Biochemistry. 2000 Mar 14;39(10):2475-83. PMID:10704197<ref>PMID:10704197</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1dm5" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Annexin 3D structures|Annexin 3D structures]] | *[[Annexin 3D structures|Annexin 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Hydra vulgaris]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Cartailler | + | [[Category: Cartailler JP]] |
| - | [[Category: Haigler | + | [[Category: Haigler HT]] |
| - | [[Category: Luecke | + | [[Category: Luecke H]] |
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Current revision
ANNEXIN XII E105K HOMOHEXAMER CRYSTAL STRUCTURE
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