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New page: left|200px<br /><applet load="1i4a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i4a, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ... |
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== | ==CRYSTAL STRUCTURE OF PHOSPHORYLATION-MIMICKING MUTANT T6D OF ANNEXIN IV== | ||
Site-directed mutagenesis, electron microscopy, and X-ray crystallography | <StructureSection load='1i4a' size='340' side='right'caption='[[1i4a]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1i4a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I4A 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]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1i4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i4a OCA], [https://pdbe.org/1i4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i4a RCSB], [https://www.ebi.ac.uk/pdbsum/1i4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i4a ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ANXA4_BOVIN ANXA4_BOVIN] May play a role in alveolar type II cells through interaction with the surfactant protein SFTPA1 (SP-A). | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i4/1i4a_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1i4a ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Site-directed mutagenesis, electron microscopy, and X-ray crystallography were used to probe the structural basis of annexin IV-induced membrane aggregation and the inhibition of this property by protein kinase C phosphorylation. Site-directed mutants that either mimic (Thr6Asp, T6D) or prevent (Thr6Ala, T6A) phosphorylation of threonine 6 were produced for these studies and compared with wild-type annexin IV. In vitro assays showed that unmodified wild-type annexin IV and the T6A mutant, but not PKC-phosphorylated wild-type or the T6D mutant, promote vesicle aggregation. Electron crystallographic data of wild-type and T6D annexin IV revealed that, similar to annexin V, the annexin IV proteins form 2D trimer-based ordered arrays on phospholipid monolayers. Cryo-electron microscopic images of junctions formed between lipid vesicles in the presence of wild-type annexin IV indicated a separation distance corresponding to the thickness of two layers of membrane-bound annexin IV. In this orientation, a single layer of WT annexin IV, attached to the outer leaflet of one vesicle, would undergo face-to-face self-association with the annexin layer of a second vesicle. The 2.0-A resolution crystal structure of the T6D mutant showed that the mutation causes release of the N-terminal tail from the protein core. This change would preclude the face-to-face annexin self-association required to aggregate vesicles. The data suggest that reversible complex formation through phosphorylation and dephosphorylation could occur in vivo and play a role in the regulation of vesicle trafficking following changes in physiological states. | |||
Phosphorylation mutants elucidate the mechanism of annexin IV-mediated membrane aggregation.,Kaetzel MA, Mo YD, Mealy TR, Campos B, Bergsma-Schutter W, Brisson A, Dedman JR, Seaton BA Biochemistry. 2001 Apr 3;40(13):4192-9. PMID:11300800<ref>PMID:11300800</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1i4a" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Annexin 3D structures|Annexin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Bergsma-Schutter | [[Category: Bergsma-Schutter W]] | ||
[[Category: Brisson | [[Category: Brisson A]] | ||
[[Category: Campos | [[Category: Campos B]] | ||
[[Category: Dedman | [[Category: Dedman JR]] | ||
[[Category: Kaetzel | [[Category: Kaetzel MA]] | ||
[[Category: Mealy | [[Category: Mealy TR]] | ||
[[Category: Mo | [[Category: Mo YD]] | ||
[[Category: Seaton | [[Category: Seaton BA]] | ||
Latest revision as of 09:21, 9 August 2023
CRYSTAL STRUCTURE OF PHOSPHORYLATION-MIMICKING MUTANT T6D OF ANNEXIN IVCRYSTAL STRUCTURE OF PHOSPHORYLATION-MIMICKING MUTANT T6D OF ANNEXIN IV
Structural highlights
FunctionANXA4_BOVIN May play a role in alveolar type II cells through interaction with the surfactant protein SFTPA1 (SP-A). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSite-directed mutagenesis, electron microscopy, and X-ray crystallography were used to probe the structural basis of annexin IV-induced membrane aggregation and the inhibition of this property by protein kinase C phosphorylation. Site-directed mutants that either mimic (Thr6Asp, T6D) or prevent (Thr6Ala, T6A) phosphorylation of threonine 6 were produced for these studies and compared with wild-type annexin IV. In vitro assays showed that unmodified wild-type annexin IV and the T6A mutant, but not PKC-phosphorylated wild-type or the T6D mutant, promote vesicle aggregation. Electron crystallographic data of wild-type and T6D annexin IV revealed that, similar to annexin V, the annexin IV proteins form 2D trimer-based ordered arrays on phospholipid monolayers. Cryo-electron microscopic images of junctions formed between lipid vesicles in the presence of wild-type annexin IV indicated a separation distance corresponding to the thickness of two layers of membrane-bound annexin IV. In this orientation, a single layer of WT annexin IV, attached to the outer leaflet of one vesicle, would undergo face-to-face self-association with the annexin layer of a second vesicle. The 2.0-A resolution crystal structure of the T6D mutant showed that the mutation causes release of the N-terminal tail from the protein core. This change would preclude the face-to-face annexin self-association required to aggregate vesicles. The data suggest that reversible complex formation through phosphorylation and dephosphorylation could occur in vivo and play a role in the regulation of vesicle trafficking following changes in physiological states. Phosphorylation mutants elucidate the mechanism of annexin IV-mediated membrane aggregation.,Kaetzel MA, Mo YD, Mealy TR, Campos B, Bergsma-Schutter W, Brisson A, Dedman JR, Seaton BA Biochemistry. 2001 Apr 3;40(13):4192-9. PMID:11300800[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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