1w8s

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(New page: 200px<br /> <applet load="1w8s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w8s, resolution 1.85&Aring;" /> '''THE MECHANISM OF TH...)
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==About this Structure==
==About this Structure==
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1W8S is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]] with FBP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W8S OCA]].
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1W8S is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Thermoproteus_tenax Thermoproteus tenax]] with FBP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Fructose-bisphosphate_aldolase Fructose-bisphosphate aldolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.13 4.1.2.13]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W8S OCA]].
==Reference==
==Reference==
Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates., Lorentzen E, Siebers B, Hensel R, Pohl E, Biochemistry. 2005 Mar 22;44(11):4222-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15766250 15766250]
Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates., Lorentzen E, Siebers B, Hensel R, Pohl E, Biochemistry. 2005 Mar 22;44(11):4222-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15766250 15766250]
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[[Category: Fructose-bisphosphate aldolase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermoproteus tenax]]
[[Category: Thermoproteus tenax]]
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[[Category: tim barrel]]
[[Category: tim barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 21:23:21 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:58:47 2007''

Revision as of 11:54, 30 October 2007


1w8s, resolution 1.85Å

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THE MECHANISM OF THE SCHIFF BASE FORMING FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE: STRUCTURAL ANALYSIS OF REACTION INTERMEDIATES

Overview

The glycolytic enzyme fructose-1,6-bisphosphate aldolase (FBPA) catalyzes, the reversible cleavage of fructose 1,6-bisphosphate to glyceraldehyde, 3-phosphate and dihydroxyacetone phosphate. Catalysis of Schiff base, forming class I FBPA relies on a number of intermediates covalently bound, to the catalytic lysine. Using active site mutants of FBPA I from, Thermoproteus tenax, we have solved the crystal structures of the enzyme, covalently bound to the carbinolamine of the substrate fructose, 1,6-bisphosphate and noncovalently bound to the cyclic form of the, substrate. The structures, determined at a resolution of 1.9 A and refined, to crystallographic R factors of 0.148 and 0.149, respectively, represent, the first view of any FBPA I in these two stages of the reaction pathway, and ... [(full description)]

About this Structure

1W8S is a [Single protein] structure of sequence from [Thermoproteus tenax] with FBP as [ligand]. Active as [Fructose-bisphosphate aldolase], with EC number [4.1.2.13]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Mechanism of the Schiff base forming fructose-1,6-bisphosphate aldolase: structural analysis of reaction intermediates., Lorentzen E, Siebers B, Hensel R, Pohl E, Biochemistry. 2005 Mar 22;44(11):4222-9. PMID:15766250

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