1cnu: Difference between revisions
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<StructureSection load='1cnu' size='340' side='right'caption='[[1cnu]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='1cnu' size='340' side='right'caption='[[1cnu]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cnu]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1cnu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acapo Acapo]. 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> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 16:10, 13 October 2021
PHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGAPHOSPHORYLATED ACTOPHORIN FROM ACANTAMOEBA POLYPHAGA
Structural highlights
Function[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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAcanthamoeba 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. 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:9737968[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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