2fgh
From Proteopedia
(New page: 200px<br /><applet load="2fgh" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fgh, resolution 2.800Å" /> '''ATP bound gelsolin'...) |
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| - | [[Image:2fgh.gif|left|200px]]<br /><applet load="2fgh" size=" | + | [[Image:2fgh.gif|left|200px]]<br /><applet load="2fgh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fgh, resolution 2.800Å" /> | caption="2fgh, resolution 2.800Å" /> | ||
'''ATP bound gelsolin'''<br /> | '''ATP bound gelsolin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Calcium activation of the actin-modifying properties of gelsolin is | + | Calcium activation of the actin-modifying properties of gelsolin is sensitive to ATP. Here, we show that soaking calcium-free gelsolin crystals in ATP-containing media results in ATP occupying a site that spans the two pseudosymmetrical halves of the protein. ATP binding involves numerous polar and hydrophobic contacts and is identical for the two copies of gelsolin related by non-crystallographic symmetry within the crystal. The gamma-phosphate of ATP participates in several charge-charge interactions consistent with the preference of gelsolin for ATP, as a binding partner, over ADP. In addition, disruption of the ATP-binding site through Ca2+ activation of gelsolin reveals why ATP binds more tightly to the inactive molecule, and suggests how the binding of ATP may modulate the sensitivity of gelsolin to calcium ions. Similarities between the ATP and PIP2 interactions with the C-terminal half of gelsolin are evident from their overlapping binding sites and in that both molecules bind more tightly in the absence of calcium ions. We propose a model for how PIP2 may bind to calcium-free gelsolin based on the ATP-binding site. |
==About this Structure== | ==About this Structure== | ||
| - | 2FGH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with ATP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2FGH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FGH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Burtnick, L | + | [[Category: Burtnick, L D.]] |
[[Category: Ma, Q.]] | [[Category: Ma, Q.]] | ||
| - | [[Category: Robinson, R | + | [[Category: Robinson, R C.]] |
[[Category: Urosev, D.]] | [[Category: Urosev, D.]] | ||
[[Category: ATP]] | [[Category: ATP]] | ||
[[Category: gelsolin; atp]] | [[Category: gelsolin; atp]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:10 2008'' |
Revision as of 15:21, 21 February 2008
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ATP bound gelsolin
Overview
Calcium activation of the actin-modifying properties of gelsolin is sensitive to ATP. Here, we show that soaking calcium-free gelsolin crystals in ATP-containing media results in ATP occupying a site that spans the two pseudosymmetrical halves of the protein. ATP binding involves numerous polar and hydrophobic contacts and is identical for the two copies of gelsolin related by non-crystallographic symmetry within the crystal. The gamma-phosphate of ATP participates in several charge-charge interactions consistent with the preference of gelsolin for ATP, as a binding partner, over ADP. In addition, disruption of the ATP-binding site through Ca2+ activation of gelsolin reveals why ATP binds more tightly to the inactive molecule, and suggests how the binding of ATP may modulate the sensitivity of gelsolin to calcium ions. Similarities between the ATP and PIP2 interactions with the C-terminal half of gelsolin are evident from their overlapping binding sites and in that both molecules bind more tightly in the absence of calcium ions. We propose a model for how PIP2 may bind to calcium-free gelsolin based on the ATP-binding site.
About this Structure
2FGH is a Single protein structure of sequence from Equus caballus with as ligand. Full crystallographic information is available from OCA.
Reference
The structure of gelsolin bound to ATP., Urosev D, Ma Q, Tan AL, Robinson RC, Burtnick LD, J Mol Biol. 2006 Mar 31;357(3):765-72. Epub 2006 Jan 25. PMID:16469333
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