1i4a: Difference between revisions
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|PDB= 1i4a |SIZE=350|CAPTION= <scene name='initialview01'>1i4a</scene>, resolution 2.0Å | |PDB= 1i4a |SIZE=350|CAPTION= <scene name='initialview01'>1i4a</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1i4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i4a OCA], [http://www.ebi.ac.uk/pdbsum/1i4a PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1i4a RCSB]</span> | |||
}} | }} | ||
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[[Category: Mo, Y D.]] | [[Category: Mo, Y D.]] | ||
[[Category: Seaton, B A.]] | [[Category: Seaton, B A.]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
[[Category: membrane-binding]] | [[Category: membrane-binding]] | ||
[[Category: phosphorylation mutant]] | [[Category: phosphorylation mutant]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:14:23 2008'' | ||
Revision as of 21:14, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF PHOSPHORYLATION-MIMICKING MUTANT T6D OF ANNEXIN IV
OverviewOverview
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.
About this StructureAbout this Structure
1I4A is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
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
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