1y64

From Proteopedia

(Difference between revisions)

Revision as of 06:27, 25 April 2018

Bni1p Formin Homology 2 Domain complexed with ATP-actin

Structural highlights

1y64 is a 2 chain structure with sequence from Atcc 18824 and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	1ux4, 1ux5
Gene:	BNI1, PPF3, SHE5 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. [BNI1_YEAST] Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and acts as leaky capper, slowing both polymerization and depolymerization. Protects the growing actin fiber from tight capping proteins and so increases the time of elongation and the total amount of F-actin. May organize microtubules by mediating spindle positioning and movement in the budding process. Potential target of the RHO family members.^[1] ^[2]

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

The conserved formin homology 2 (FH2) domain nucleates actin filaments and remains bound to the barbed end of the growing filament. Here we report the crystal structure of the yeast Bni1p FH2 domain in complex with tetramethylrhodamine-actin. Each of the two structural units in the FH2 dimer binds two actins in an orientation similar to that in an actin filament, suggesting that this structure could function as a filament nucleus. Biochemical properties of heterodimeric FH2 mutants suggest that the wild-type protein equilibrates between two bound states at the barbed end: one permitting monomer binding and the other permitting monomer dissociation. Interconversion between these states allows processive barbed-end polymerization and depolymerization in the presence of bound FH2 domain. Kinetic and/or thermodynamic differences in the conformational and binding equilibria can explain the variable activity of different FH2 domains as well as the effects of the actin-binding protein profilin on FH2 function.

Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain.,Otomo T, Tomchick DR, Otomo C, Panchal SC, Machius M, Rosen MK Nature. 2005 Feb 3;433(7025):488-94. Epub 2005 Jan 5. PMID:15635372^[3]

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

References

↑ Lee L, Klee SK, Evangelista M, Boone C, Pellman D. Control of mitotic spindle position by the Saccharomyces cerevisiae formin Bni1p. J Cell Biol. 1999 Mar 8;144(5):947-61. PMID:10085293
↑ Zigmond SH, Evangelista M, Boone C, Yang C, Dar AC, Sicheri F, Forkey J, Pring M. Formin leaky cap allows elongation in the presence of tight capping proteins. Curr Biol. 2003 Oct 14;13(20):1820-3. PMID:14561409
↑ Otomo T, Tomchick DR, Otomo C, Panchal SC, Machius M, Rosen MK. Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature. 2005 Feb 3;433(7025):488-94. Epub 2005 Jan 5. PMID:15635372 doi:10.1038/nature03251

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1y64"

@@ Line 1: / Line 1: @@
 ==Bni1p Formin Homology 2 Domain complexed with ATP-actin==
 <StructureSection load='1y64' size='340' side='right' caption='[[1y64]], [[Resolution|resolution]] 3.05&Aring;' scene=''>
@@ Line 7: / Line 8: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ux4|1ux4]], [[1ux5|1ux5]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BNI1, PPF3, SHE5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=1y64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y64 OCA], [http://pdbe.org/1y64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y64 RCSB], [http://www.ebi.ac.uk/pdbsum/1y64 PDBsum]</span></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=1y64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y64 OCA], [http://pdbe.org/1y64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y64 RCSB], [http://www.ebi.ac.uk/pdbsum/1y64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y64 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 15: / Line 16: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y6/1y64_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/y6/1y64_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 47: / Line 48: @@
 [[Category: Actin]]
 [[Category: Atp-state]]
+[[Category: Coiled coil]]
 [[Category: Fh2 actin cytoskeleton]]
 [[Category: Structural protein]]
 [[Category: Tetramethylrhodamine-5-maleimide]]

1y64

From Proteopedia

Revision as of 06:27, 25 April 2018

Bni1p Formin Homology 2 Domain complexed with ATP-actin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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