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[[Image:1acf.gif|left|200px]]


{{Structure
==ACANTHAMOEBA CASTELLANII PROFILIN IB==
|PDB= 1acf |SIZE=350|CAPTION= <scene name='initialview01'>1acf</scene>, resolution 2.0&Aring;
<StructureSection load='1acf' size='340' side='right'caption='[[1acf]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1acf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ACF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ACF FirstGlance]. <br>
|ACTIVITY=  
</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&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1acf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1acf OCA], [https://pdbe.org/1acf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1acf RCSB], [https://www.ebi.ac.uk/pdbsum/1acf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1acf ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1acf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1acf OCA], [http://www.ebi.ac.uk/pdbsum/1acf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1acf RCSB]</span>
[https://www.uniprot.org/uniprot/PRO1B_ACACA PRO1B_ACACA] Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.
}}
== 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/ac/1acf_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=1acf ConSurf].
<div style="clear:both"></div>


'''ACANTHAMOEBA CASTELLANII PROFILIN IB'''
==See Also==
 
*[[Profilin 3D Structures|Profilin 3D Structures]]
 
__TOC__
==Overview==
</StructureSection>
We determined the structures of Acanthamoeba profilin I and profilin II by x-ray crystallography at resolutions of 2.0 and 2.8 A, respectively. The polypeptide folds and the actin-binding surfaces of the amoeba profilins are very similar to those of bovine and human profilins. The electrostatic potential surfaces of the two Acanthamoeba isoforms differ. Two areas of high positive potential on the surface of profilin II are candidate binding sites for phosphatidylinositol phosphates. The proximity of these sites to the actin binding site provides an explanation for the competition between actin and lipids for binding profilin.
 
==About this Structure==
1ACF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_castellanii Acanthamoeba castellanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ACF OCA].
 
==Reference==
X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates., Fedorov AA, Magnus KA, Graupe MH, Lattman EE, Pollard TD, Almo SC, Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8636-40. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8078936 8078936]
[[Category: Acanthamoeba castellanii]]
[[Category: Acanthamoeba castellanii]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Almo, S C.]]
[[Category: Almo SC]]
[[Category: Fedorov, A A.]]
[[Category: Fedorov AA]]
[[Category: Graupe, M H.]]
[[Category: Graupe MH]]
[[Category: Lattman, E E.]]
[[Category: Lattman EE]]
[[Category: Magnus, K A.]]
[[Category: Magnus KA]]
[[Category: Pollard, T D.]]
[[Category: Pollard TD]]
[[Category: actin-binding protein]]
[[Category: profilin]]
[[Category: protein binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:37:27 2008''

Latest revision as of 09:29, 7 February 2024

ACANTHAMOEBA CASTELLANII PROFILIN IBACANTHAMOEBA CASTELLANII PROFILIN IB

Structural highlights

1acf is a 1 chain structure with sequence from Acanthamoeba castellanii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PRO1B_ACACA Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1acf, resolution 2.00Å

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