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6b3i

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Annexin A13a

Structural highlights

6b3i is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ANX13_HUMAN Binds to membranes enriched in phosphatidylserine or phosphatidylglycerol in a calcium-dependent manner (PubMed:27676605, PubMed:30610115). Half-maximal membrane binding requires about 60 uM calcium. Does not bind to membranes that lack phospholipids with an acidic headgroup (PubMed:27676605).^[1] ^[2] Binds to membranes enriched in phosphatidylserine or phosphatidylglycerol in a calcium-dependent manner, but requires higher calcium levels for membrane binding than isoform A. Half-maximal membrane binding requires about 320 uM calcium.^[3]

Publication Abstract from PubMed

Annexin proteins function as Ca(2+)-dependent regulators of membrane trafficking and repair that may also modulate membrane curvature. Here, using high-resolution confocal imaging, we report that the intestine-specific annexin A13 (ANX A13) localizes to the tips of intestinal microvilli and determined the crystal structure of the ANX A13a isoform to 2.6 A resolution. The structure revealed that the N terminus exhibits an alternative fold that converts the first two helices and the associated helix-loop-helix motif into a continuous alpha-helix, as stabilized by a domain-swapped dimer. We also found that the dimer is present in solution and partially occludes the membrane-binding surfaces of annexin, suggesting that dimerization may function as a means for regulating membrane binding. Accordingly, as revealed by in vitro binding and cellular localization assays, ANX A13a variants that favor a monomeric state exhibited increased membrane association relative to variants that favor the dimeric form. Together, our findings support a mechanism for how the association of the ANX A13a isoform with the membrane is regulated.

An alternative N-terminal fold of the intestine-specific annexin A13a induces dimerization and regulates membrane-binding.,McCulloch KM, Yamakawa I, Shifrin DA Jr, McConnell RE, Foegeding NJ, Singh PK, Mao S, Tyska MJ, Iverson TM J Biol Chem. 2019 Mar 8;294(10):3454-3463. doi: 10.1074/jbc.RA118.004571. Epub, 2019 Jan 4. PMID:30610115^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Fernández-Lizarbe S, Lecona E, Santiago-Gómez A, Olmo N, Lizarbe MA, Turnay J. Structural and lipid-binding characterization of human annexin A13a reveals strong differences with its long A13b isoform. Biol Chem. 2017 Mar;398(3):359-371. PMID:27676605 doi:10.1515/hsz-2016-0242
↑ McCulloch KM, Yamakawa I, Shifrin DA Jr, McConnell RE, Foegeding NJ, Singh PK, Mao S, Tyska MJ, Iverson TM. An alternative N-terminal fold of the intestine-specific annexin A13a induces dimerization and regulates membrane-binding. J Biol Chem. 2019 Mar 8;294(10):3454-3463. doi: 10.1074/jbc.RA118.004571. Epub, 2019 Jan 4. PMID:30610115 doi:http://dx.doi.org/10.1074/jbc.RA118.004571
↑ Fernández-Lizarbe S, Lecona E, Santiago-Gómez A, Olmo N, Lizarbe MA, Turnay J. Structural and lipid-binding characterization of human annexin A13a reveals strong differences with its long A13b isoform. Biol Chem. 2017 Mar;398(3):359-371. PMID:27676605 doi:10.1515/hsz-2016-0242
↑ McCulloch KM, Yamakawa I, Shifrin DA Jr, McConnell RE, Foegeding NJ, Singh PK, Mao S, Tyska MJ, Iverson TM. An alternative N-terminal fold of the intestine-specific annexin A13a induces dimerization and regulates membrane-binding. J Biol Chem. 2019 Mar 8;294(10):3454-3463. doi: 10.1074/jbc.RA118.004571. Epub, 2019 Jan 4. PMID:30610115 doi:http://dx.doi.org/10.1074/jbc.RA118.004571

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6b3i"

Categories: Homo sapiens | Large Structures | Iverson TM | McCulloch KM

@@ Line 3: / Line 3: @@
 <StructureSection load='6b3i' size='340' side='right'caption='[[6b3i]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6b3i]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B3I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6B3I FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6b3i]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6B3I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6B3I FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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]] 2.6&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ANXA13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-<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=6b3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b3i OCA], [http://pdbe.org/6b3i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6b3i RCSB], [http://www.ebi.ac.uk/pdbsum/6b3i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6b3i 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=6b3i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6b3i OCA], [https://pdbe.org/6b3i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6b3i RCSB], [https://www.ebi.ac.uk/pdbsum/6b3i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6b3i ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ANX13_HUMAN ANX13_HUMAN] Binds to membranes enriched in phosphatidylserine or phosphatidylglycerol in a calcium-dependent manner (PubMed:27676605, PubMed:30610115). Half-maximal membrane binding requires about 60 uM calcium. Does not bind to membranes that lack phospholipids with an acidic headgroup (PubMed:27676605).<ref>PMID:27676605</ref> <ref>PMID:30610115</ref>   Binds to membranes enriched in phosphatidylserine or phosphatidylglycerol in a calcium-dependent manner, but requires higher calcium levels for membrane binding than isoform A. Half-maximal membrane binding requires about 320 uM calcium.<ref>PMID:27676605</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Iverson, T M]]
+[[Category: Iverson TM]]
-[[Category: McCulloch, K M]]
+[[Category: McCulloch KM]]
-[[Category: Annexin]]
-[[Category: Lipid binding protein]]

6b3i

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Current revision

Annexin A13a

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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