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1svy
From Proteopedia
(New page: 200px<br /><applet load="1svy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1svy, resolution 1.75Å" /> '''SEVERIN DOMAIN 2, 1....) |
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| - | [[Image:1svy.gif|left|200px]]<br /><applet load="1svy" size=" | + | [[Image:1svy.gif|left|200px]]<br /><applet load="1svy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1svy, resolution 1.75Å" /> | caption="1svy, resolution 1.75Å" /> | ||
'''SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE'''<br /> | '''SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the F-actin binding domain 2 of severin, the | + | The crystal structure of the F-actin binding domain 2 of severin, the gelsolin homologue from Dictyostelium discoideum, has been determined by multiple isomorphous replacement and refined to 1.75 A resolution. The structure reveals an alpha-helix-beta-sheet sandwich similar to the domains of gelsolin and villin, and contains two cation-binding sites, as observed in other domain 1 and domain 2 homologues. Comparison of the structures of several gelsolin family domains has identified residues that may mediate F-actin binding in gelsolin domain 2 homologues. To assess the involvement of these residues in F-actin binding, three mutants of human gelsolin domain 2 were assayed for F-actin binding activity and thermodynamic stability. Two of the mutants, RRV168AAA and RLK210AAA, demonstrated a lowered affinity for F-actin, indicating a role for those residues in filament binding. Using both structural and biochemical data, we have constructed a model of the gelsolin domain 1-domain 2-F-actin complex. This model highlights a number of interactions that may serve as positive and negative determinants of filament end- and side-binding. |
==About this Structure== | ==About this Structure== | ||
| - | 1SVY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with CA and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1SVY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SVY OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Dictyostelium discoideum]] | [[Category: Dictyostelium discoideum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Almo, S | + | [[Category: Almo, S C.]] |
[[Category: Eichinger, L.]] | [[Category: Eichinger, L.]] | ||
| - | [[Category: Fedorov, E | + | [[Category: Fedorov, E V.]] |
| - | [[Category: Puius, Y | + | [[Category: Puius, Y A.]] |
[[Category: Schleicher, M.]] | [[Category: Schleicher, M.]] | ||
[[Category: Sullivan, M.]] | [[Category: Sullivan, M.]] | ||
| Line 30: | Line 30: | ||
[[Category: villin]] | [[Category: villin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:05:46 2008'' |
Revision as of 13:05, 21 February 2008
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SEVERIN DOMAIN 2, 1.75 ANGSTROM CRYSTAL STRUCTURE
Overview
The crystal structure of the F-actin binding domain 2 of severin, the gelsolin homologue from Dictyostelium discoideum, has been determined by multiple isomorphous replacement and refined to 1.75 A resolution. The structure reveals an alpha-helix-beta-sheet sandwich similar to the domains of gelsolin and villin, and contains two cation-binding sites, as observed in other domain 1 and domain 2 homologues. Comparison of the structures of several gelsolin family domains has identified residues that may mediate F-actin binding in gelsolin domain 2 homologues. To assess the involvement of these residues in F-actin binding, three mutants of human gelsolin domain 2 were assayed for F-actin binding activity and thermodynamic stability. Two of the mutants, RRV168AAA and RLK210AAA, demonstrated a lowered affinity for F-actin, indicating a role for those residues in filament binding. Using both structural and biochemical data, we have constructed a model of the gelsolin domain 1-domain 2-F-actin complex. This model highlights a number of interactions that may serve as positive and negative determinants of filament end- and side-binding.
About this Structure
1SVY is a Single protein structure of sequence from Dictyostelium discoideum with and as ligands. Full crystallographic information is available from OCA.
Reference
Mapping the functional surface of domain 2 in the gelsolin superfamily., Puius YA, Fedorov EV, Eichinger L, Schleicher M, Almo SC, Biochemistry. 2000 May 9;39(18):5322-31. PMID:10820002
Page seeded by OCA on Thu Feb 21 15:05:46 2008
Categories: Dictyostelium discoideum | Single protein | Almo, S C. | Eichinger, L. | Fedorov, E V. | Puius, Y A. | Schleicher, M. | Sullivan, M. | CA | NA | Actin-binding protein | Calcium | Calcium-binding | Cytoskeleton | Gelsolin | Pip2 | Severin | Villin
