1acf: Difference between revisions

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[[Image:1acf.png|left|200px]]
==ACANTHAMOEBA CASTELLANII PROFILIN IB==
<StructureSection load='1acf' size='340' side='right' caption='[[1acf]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1acf]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ACF FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1acf RCSB], [http://www.ebi.ac.uk/pdbsum/1acf PDBsum]</span></td></tr>
<table>
== 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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


{{STRUCTURE_1acf|  PDB=1acf  |  SCENE=  }}
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:8078936<ref>PMID:8078936</ref>


===ACANTHAMOEBA CASTELLANII PROFILIN IB===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_8078936}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[1acf]] is a 1 chain structure with 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].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:008078936</ref><references group="xtra"/>
[[Category: Acanthamoeba castellanii]]
[[Category: Acanthamoeba castellanii]]
[[Category: Almo, S C.]]
[[Category: Almo, S C.]]

Revision as of 11:27, 23 July 2014

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.
Resources:FirstGlance, OCA, RCSB, PDBsum

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

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.

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:8078936[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Fedorov AA, Magnus KA, Graupe MH, Lattman EE, Pollard TD, Almo SC. X-ray structures of isoforms of the actin-binding protein profilin that differ in their affinity for phosphatidylinositol phosphates. Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8636-40. PMID:8078936

1acf, resolution 2.00Å

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