1i4a: Difference between revisions

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[[Image:1i4a.gif|left|200px]]<br /><applet load="1i4a" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1i4a.gif|left|200px]]
caption="1i4a, resolution 2.0&Aring;" />
 
'''CRYSTAL STRUCTURE OF PHOSPHORYLATION-MIMICKING MUTANT T6D OF ANNEXIN IV'''<br />
{{Structure
|PDB= 1i4a |SIZE=350|CAPTION= <scene name='initialview01'>1i4a</scene>, resolution 2.0&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|ACTIVITY=
|GENE=
}}
 
'''CRYSTAL STRUCTURE OF PHOSPHORYLATION-MIMICKING MUTANT T6D OF ANNEXIN IV'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1I4A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I4A OCA].  
1I4A is a [[Single protein]] structure of sequence from [http://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].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11300800 11300800]
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:[http://www.ncbi.nlm.nih.gov/pubmed/11300800 11300800]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: phosphorylation mutant]]
[[Category: phosphorylation mutant]]


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Revision as of 12:45, 20 March 2008

File:1i4a.gif


PDB ID 1i4a

Drag the structure with the mouse to rotate
, resolution 2.0Å
Ligands: and
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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