1o7x

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(New page: 200px<br /><applet load="1o7x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o7x, resolution 2.7&Aring;" /> '''CITRATE SYNTHASE FROM...)
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[[Image:1o7x.jpg|left|200px]]<br /><applet load="1o7x" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1o7x, resolution 2.7&Aring;" />
caption="1o7x, resolution 2.7&Aring;" />
'''CITRATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS'''<br />
'''CITRATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS'''<br />
==Overview==
==Overview==
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The crystal structure of citrate synthase from the thermophilic Archaeon, Sulfolobus solfataricus (optimum growth temperature = 85 degrees C) has, been determined, extending the number of crystal structures of citrate, synthase from different organisms to a total of five that span the, temperature range over which life exists (from psychrophile to, hyperthermophile). Detailed structural analysis has revealed possible, molecular mechanisms that determine the different stabilities of the five, proteins. The key to these mechanisms is the precise structural location, of the additional interactions. As one ascends the temperature ladder, the, subunit interface of this dimeric enzyme and loop regions are reinforced, by complex electrostatic interactions, and there is a reduced exposure of, hydrophobic surface. These observations reveal a progressive pattern of, stabilization through multiple additional interactions at solvent exposed, loop and interfacial regions.
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The crystal structure of citrate synthase from the thermophilic Archaeon Sulfolobus solfataricus (optimum growth temperature = 85 degrees C) has been determined, extending the number of crystal structures of citrate synthase from different organisms to a total of five that span the temperature range over which life exists (from psychrophile to hyperthermophile). Detailed structural analysis has revealed possible molecular mechanisms that determine the different stabilities of the five proteins. The key to these mechanisms is the precise structural location of the additional interactions. As one ascends the temperature ladder, the subunit interface of this dimeric enzyme and loop regions are reinforced by complex electrostatic interactions, and there is a reduced exposure of hydrophobic surface. These observations reveal a progressive pattern of stabilization through multiple additional interactions at solvent exposed, loop and interfacial regions.
==About this Structure==
==About this Structure==
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1O7X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Active as [http://en.wikipedia.org/wiki/Citrate_(Si)-synthase Citrate (Si)-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.1 2.3.3.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O7X OCA].
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1O7X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Active as [http://en.wikipedia.org/wiki/Citrate_(Si)-synthase Citrate (Si)-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.3.1 2.3.3.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7X OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sulfolobus solfataricus]]
[[Category: Sulfolobus solfataricus]]
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[[Category: Bell, G.S.]]
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[[Category: Bell, G S.]]
[[Category: Connaris, H.]]
[[Category: Connaris, H.]]
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[[Category: Danson, M.J.]]
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[[Category: Danson, M J.]]
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[[Category: Hough, D.W.]]
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[[Category: Hough, D W.]]
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[[Category: Russell, R.J.M.]]
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[[Category: Russell, R J.M.]]
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[[Category: Taylor, G.L.]]
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[[Category: Taylor, G L.]]
[[Category: lyase]]
[[Category: lyase]]
[[Category: tricarboxylic acid cycle]]
[[Category: tricarboxylic acid cycle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:52:02 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:14:28 2008''

Revision as of 12:14, 21 February 2008


1o7x, resolution 2.7Å

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CITRATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS

Overview

The crystal structure of citrate synthase from the thermophilic Archaeon Sulfolobus solfataricus (optimum growth temperature = 85 degrees C) has been determined, extending the number of crystal structures of citrate synthase from different organisms to a total of five that span the temperature range over which life exists (from psychrophile to hyperthermophile). Detailed structural analysis has revealed possible molecular mechanisms that determine the different stabilities of the five proteins. The key to these mechanisms is the precise structural location of the additional interactions. As one ascends the temperature ladder, the subunit interface of this dimeric enzyme and loop regions are reinforced by complex electrostatic interactions, and there is a reduced exposure of hydrophobic surface. These observations reveal a progressive pattern of stabilization through multiple additional interactions at solvent exposed, loop and interfacial regions.

About this Structure

1O7X is a Single protein structure of sequence from Sulfolobus solfataricus. Active as Citrate (Si)-synthase, with EC number 2.3.3.1 Full crystallographic information is available from OCA.

Reference

Stepwise adaptations of citrate synthase to survival at life's extremes. From psychrophile to hyperthermophile., Bell GS, Russell RJ, Connaris H, Hough DW, Danson MJ, Taylor GL, Eur J Biochem. 2002 Dec;269(24):6250-60. PMID:12473121

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