View source for 3byh


==Model of actin-fimbrin ABD2 complex==
<SX load='3byh' size='340' side='right' viewer='molstar' caption='[[3byh]], [[Resolution|resolution]] 12.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3byh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BYH FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PS1TP5BP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3byh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3byh OCA], [http://pdbe.org/3byh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3byh RCSB], [http://www.ebi.ac.uk/pdbsum/3byh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3byh ProSAT]</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/by/3byh_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=3byh ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
Many actin binding proteins have a modular architecture, and calponin-homology (CH) domains are one such structurally conserved module found in numerous proteins that interact with F-actin. The manner in which CH-domains bind F-actin has been controversial. Using cryo-EM and a single-particle approach to helical reconstruction, we have generated 12-A-resolution maps of F-actin alone and F-actin decorated with a fragment of human fimbrin (L-plastin) containing tandem CH-domains. The high resolution allows an unambiguous fit of the crystal structure of fimbrin into the map. The interaction between fimbrin ABD2 (actin binding domain 2) and F-actin is different from any interaction previously observed or proposed for tandem CH-domain proteins, showing that the structural conservation of the CH-domains does not lead to a conserved mode of interaction with F-actin. Both the stapling of adjacent actin protomers and the additional closure of the nucleotide binding cleft in F-actin when the fimbrin fragment binds may explain how fimbrin can stabilize actin filaments. A mechanism is proposed where ABD1 of fimbrin becomes activated for binding a second actin filament after ABD2 is bound to a first filament, and this can explain how mutations of residues buried in the interface between ABD2 and ABD1 can rescue temperature-sensitive defects in actin.

High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex.,Galkin VE, Orlova A, Cherepanova O, Lebart MC, Egelman EH Proc Natl Acad Sci U S A. 2008 Feb 5;105(5):1494-8. Epub 2008 Jan 30. PMID:18234857<ref>PMID:18234857</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3byh" style="background-color:#fffaf0;"></div>

==See Also==
*[[Actin 3D structures|Actin 3D structures]]
== References ==
<references/>
__TOC__
</SX>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Cherepanova, O]]
[[Category: Egelman, E H]]
[[Category: Galkin, V E]]
[[Category: Lebart, M C]]
[[Category: Orlova, A]]
[[Category: Acetylation]]
[[Category: Atp-binding]]
[[Category: Cytoplasm]]
[[Category: Cytoskeleton]]
[[Category: Helical filament]]
[[Category: Methylation]]
[[Category: Nucleotide-binding]]
[[Category: Phosphoprotein]]
[[Category: Protein polymer]]
[[Category: Structural protein]]