This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1cnu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1cnu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cnu, resolution 2.25&Aring;" /> '''PHOSPHORYLATED ACTOP...)
Current revision (06:44, 7 February 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1cnu.gif|left|200px]]<br /><applet load="1cnu" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1cnu, resolution 2.25&Aring;" />
 
-
'''PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA'''<br />
 
-
==Overview==
+
==PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA==
-
Acanthamoeba actophorin is a member of ADF/cofilin family that binds both, actin monomers and filaments. We used fluorescence anisotropy to study the, interaction of actin monomers with recombinant actophorin labeled with, rhodamine on a cysteine substituted for Serine-88. Labeled actophorin, retains its affinity for actin and ability to reduce the low shear, viscosity of actin filaments. At physiological ionic strength, actophorin, binds Mg-ADP-actin monomers (Kd = 0.1 microM) 40 times stronger than, Mg-ATP-actin monomers. When bound to actin monomers, actophorin has no, effect on elongation at either end of actin filaments by Mg-ATP-actin and, slightly increases the rate of elongation at both ends by Mg-ADP-actin., Thus actophorin does not sequester actin monomers. Sedimentation, equilibrium ultracentrifugation shows that actophorin and profilin compete, for binding actin monomers. Actophorin and profilin have opposite effects, on the rate of exchange of nucleotide bound to actin monomers. Despite the, high affinity of actophorin for ADP-actin, physiological concentrations of, profilin overcome the inhibition of ADP exchange by actophorin. Profilin, rapidly recycles ADP-actin back to the profilin-ATP-actin pool ready for, elongation of actin filaments.
+
<StructureSection load='1cnu' size='340' side='right'caption='[[1cnu]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
-
 
+
== Structural highlights ==
-
==About this Structure==
+
<table><tr><td colspan='2'>[[1cnu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthamoeba_polyphaga Acanthamoeba polyphaga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CNU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CNU FirstGlance]. <br>
-
1CNU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Acanthamoeba_polyphaga Acanthamoeba polyphaga]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CNU OCA].
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
-
 
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
-
==Reference==
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cnu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cnu OCA], [https://pdbe.org/1cnu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cnu RCSB], [https://www.ebi.ac.uk/pdbsum/1cnu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cnu ProSAT]</span></td></tr>
-
Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin., Blanchoin L, Pollard TD, J Biol Chem. 1998 Sep 25;273(39):25106-11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9737968 9737968]
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ACTP_ACACA ACTP_ACACA] Forms a one to one complex with monomeric actin. Can regulate the pool available for polymerization. Severs actin filaments in a dose-dependent manner.
 +
== 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/cn/1cnu_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=1cnu ConSurf].
 +
<div style="clear:both"></div>
 +
__TOC__
 +
</StructureSection>
[[Category: Acanthamoeba polyphaga]]
[[Category: Acanthamoeba polyphaga]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Blanchoin, L.]]
+
[[Category: Blanchoin L]]
-
[[Category: Choe, S.]]
+
[[Category: Choe S]]
-
[[Category: Pollard, T.D.]]
+
[[Category: Pollard TD]]
-
[[Category: Robinson, R.C.]]
+
[[Category: Robinson RC]]
-
[[Category: actin-binding protein]]
+
-
[[Category: adf]]
+
-
[[Category: cofilin]]
+
-
[[Category: contractile]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:36:36 2007''
+

Current revision

PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA

PDB ID 1cnu

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cnu"
Personal tools