1i4a

CRYSTAL STRUCTURE OF PHOSPHORYLATION-MIMICKING MUTANT T6D OF ANNEXIN IV

spinqualitylabelsall models 1i4a, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1i4a is a 1 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [ANXA4_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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Annexin

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