1h1v

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[[Image:1h1v.gif|left|200px]]
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==Overview==
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{{ABSTRACT_12460571}}
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Gelsolin participates in the reorganization of the actin cytoskeleton that is required during such phenomena as cell movement, cytokinesis, and apoptosis. It consists of six structurally similar domains, G1-G6, which are arranged at resting intracellular levels of calcium ion so as to obscure the three actin-binding surfaces. Elevation of Ca(2+) concentrations releases latches within the constrained structure and produces large shifts in the relative positioning of the domains, permitting gelsolin to bind to and sever actin filaments. How Ca(2+) is able to activate gelsolin has been a major question concerning the function of this protein. We present the improved structure of the C-terminal half of gelsolin bound to monomeric actin at 3.0 A resolution. Two classes of Ca(2+)-binding site are evident on gelsolin: type 1 sites share coordination of Ca(2+) with actin, while type 2 sites are wholly contained within gelsolin. This structure of the complex reveals the locations of two novel metal ion-binding sites in domains G5 and G6, respectively. We identify both as type 2 sites. The absolute conservation of the type 2 calcium-ligating residues across the six domains of gelsolin suggests that this site exists in each of the domains. In total, gelsolin has the potential to bind eight calcium ions, two type 1 and six type 2. The function of the type 2 sites is to facilitate structural rearrangements within gelsolin as part of the activation and actin-binding and severing processes. We propose the novel type 2 site in G6 to be the critical site that initiates overall activation of gelsolin by releasing the tail latch that locks calcium-free gelsolin in a conformation unable to bind actin.
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==About this Structure==
==About this Structure==
1H1V is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1db0 1db0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1V OCA].
1H1V is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1db0 1db0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H1V OCA].
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==Reference==
 
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The calcium activation of gelsolin: insights from the 3A structure of the G4-G6/actin complex., Choe H, Burtnick LD, Mejillano M, Yin HL, Robinson RC, Choe S, J Mol Biol. 2002 Dec 6;324(4):691-702. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12460571 12460571]
 
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Muscle contraction]]
[[Category: Muscle contraction]]
[[Category: Severing]]
[[Category: Severing]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:18:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 25 19:16:05 2008''

Revision as of 16:16, 25 June 2008

Image:1h1v.png

Template:STRUCTURE 1h1v

GELSOLIN G4-G6/ACTIN COMPLEX


Template:ABSTRACT 12460571

About this Structure

1H1V is a Protein complex structure of sequences from Homo sapiens and Oryctolagus cuniculus. This structure supersedes the now removed PDB entry 1db0. Full crystallographic information is available from OCA.

Page seeded by OCA on Wed Jun 25 19:16:05 2008

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