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New page: left|200px<br /><applet load="1sjj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sjj" /> '''Cryo-EM Structure of Chicken Gizzard Smooth ...
 
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[[Image:1sjj.gif|left|200px]]<br /><applet load="1sjj" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1sjj.gif|left|200px]]<br /><applet load="1sjj" size="350" color="white" frame="true" align="right" spinBox="true"  
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'''Cryo-EM Structure of Chicken Gizzard Smooth Muscle alpha-Actinin'''<br />
'''Cryo-EM Structure of Chicken Gizzard Smooth Muscle alpha-Actinin'''<br />


==Overview==
==Overview==
Cryoelectron microscopy was used to obtain a 3-D image at 2.0 nm, resolution of 2-D arrays of smooth muscle alpha-actinin. The, reconstruction reveals a well-resolved long central domain with 90 degrees, of left-handed twist and near 2-fold symmetry. However, the molecular ends, which contain the actin binding and calmodulin-like domains, have, different structures oriented approximately 90 degrees to each other., Atomic structures for the alpha-actinin domains were built by homology, modeling and assembled into an atomic model. Model building suggests that, in the 2-D arrays, the two calponin homology domains that comprise the, actin-binding domain have a closed conformation at one end and an open, conformation at the other end due to domain swapping. The open and closed, conformations of the actin-binding domain suggests flexibility that may, underlie Ca2+ regulation. The approximately 90 degrees orientation, difference at the molecular ends may underlie alpha-actinin's ability to, crosslink actin filaments in nearly any orientation.
Cryoelectron microscopy was used to obtain a 3-D image at 2.0 nm resolution of 2-D arrays of smooth muscle alpha-actinin. The reconstruction reveals a well-resolved long central domain with 90 degrees of left-handed twist and near 2-fold symmetry. However, the molecular ends which contain the actin binding and calmodulin-like domains, have different structures oriented approximately 90 degrees to each other. Atomic structures for the alpha-actinin domains were built by homology modeling and assembled into an atomic model. Model building suggests that in the 2-D arrays, the two calponin homology domains that comprise the actin-binding domain have a closed conformation at one end and an open conformation at the other end due to domain swapping. The open and closed conformations of the actin-binding domain suggests flexibility that may underlie Ca2+ regulation. The approximately 90 degrees orientation difference at the molecular ends may underlie alpha-actinin's ability to crosslink actin filaments in nearly any orientation.


==About this Structure==
==About this Structure==
1SJJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1SJJ OCA].  
1SJJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SJJ OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Liu, J.]]
[[Category: Liu, J.]]
[[Category: Taylor, D.W.]]
[[Category: Taylor, D W.]]
[[Category: Taylor, K.A.]]
[[Category: Taylor, K A.]]
[[Category: 3-helix bundle]]
[[Category: 3-helix bundle]]
[[Category: actin binding protein]]
[[Category: actin binding protein]]
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[[Category: calponin homology domain]]
[[Category: calponin homology domain]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:02:10 2008''

Revision as of 13:02, 21 February 2008

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1sjj

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Cryo-EM Structure of Chicken Gizzard Smooth Muscle alpha-Actinin

Overview

Cryoelectron microscopy was used to obtain a 3-D image at 2.0 nm resolution of 2-D arrays of smooth muscle alpha-actinin. The reconstruction reveals a well-resolved long central domain with 90 degrees of left-handed twist and near 2-fold symmetry. However, the molecular ends which contain the actin binding and calmodulin-like domains, have different structures oriented approximately 90 degrees to each other. Atomic structures for the alpha-actinin domains were built by homology modeling and assembled into an atomic model. Model building suggests that in the 2-D arrays, the two calponin homology domains that comprise the actin-binding domain have a closed conformation at one end and an open conformation at the other end due to domain swapping. The open and closed conformations of the actin-binding domain suggests flexibility that may underlie Ca2+ regulation. The approximately 90 degrees orientation difference at the molecular ends may underlie alpha-actinin's ability to crosslink actin filaments in nearly any orientation.

About this Structure

1SJJ is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

A 3-D reconstruction of smooth muscle alpha-actinin by CryoEm reveals two different conformations at the actin-binding region., Liu J, Taylor DW, Taylor KA, J Mol Biol. 2004 Apr 16;338(1):115-25. PMID:15050827

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