View source for 5jjg


==Structure of magnesium-loaded ALG-2==
<StructureSection load='5jjg' size='340' side='right'caption='[[5jjg]], [[Resolution|resolution]] 1.72&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5jjg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JJG FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</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=5jjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jjg OCA], [https://pdbe.org/5jjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jjg RCSB], [https://www.ebi.ac.uk/pdbsum/5jjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jjg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PDCD6_MOUSE PDCD6_MOUSE] Calcium-binding protein required for T-cell receptor-, Fas-, and glucocorticoid-induced cell death. Calcium-dependent adapter necessary for the association between PDCD6IP and TSG101 (By similarity). May mediate Ca(2+)-regulated signals along the death pathway. Interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The penta-EF-hand (PEF) protein ALG-2 (apoptosis-linked gene 2) has been implicated in several important physiological processes, including endoplasmic reticulum-Golgi vesicular transport and endosomal biogenesis/transport. ALG-2 was recently shown to harbor a metal ion-binding site with a high affinity for Mg2+ and a low affinity for Ca2+. We herein present the X-ray structure of Mg2+-bound ALG-2des23wt. Although the Calpha trace is nearly indistinguishable from that of the Ca2+-free protein, the orientation of the C-terminal helix differs in the two structures. Consistent with that observation, replacement of the +x ligand in EF5, D169, with alanine eliminates high-affinity Mg2+ binding. It also eliminates the low-affinity Ca2+ site and lowers the affinity of the remaining Ca2+-binding sites, EF3 and EF1. The coordination environment in EF5 approaches ideal Mg2+ octahedral geometry. The ligand array, consisting of three carboxylates (+x, +y, +z), a backbone carbonyl (-y), and two water molecules (-x, -z), may offer a recipe for a high-affinity, high-selectivity Mg2+-binding site. Sequence data for other PEF proteins indicate that select calpain large subunits, notably CAPN1 and CAPN8, may also possess a high-affinity Mg2+-binding site. In Mg2+-bound ALG-2, the carbonyl of F188 and the C-terminal carboxylate of V191 interact with the epsilon-ammonium group of K137 in the opposing subunit, suggesting that Mg2+ binding could have an impact on dimerization. Interestingly, EF1 and EF3 are also occupied in the crystal, despite having modest affinity for Mg2+. The results of a calorimetry-based analysis indicate that their Mg2+ binding constants are 2 orders of magnitude lower than that determined for EF5.

EF5 Is the High-Affinity Mg2+ Site in ALG-2.,Tanner JJ, Frey BB, Pemberton T, Henzl MT Biochemistry. 2016 Aug 31. PMID:27541325<ref>PMID:27541325</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Tanner JJ]]