1wbh
From Proteopedia
(New page: 200px<br /> <applet load="1wbh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wbh, resolution 1.55Å" /> '''CRYSTAL STRUCTURE O...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1WBH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with PO4 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=4.1.2.14 4.1.2.14]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WBH OCA]]. | + | 1WBH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with PO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/2-dehydro-3-deoxy-phosphogluconate_aldolase 2-dehydro-3-deoxy-phosphogluconate aldolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.14 4.1.2.14]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WBH OCA]]. |
==Reference== | ==Reference== | ||
Mechanism of the Class I KDPG aldolase., Fullerton SW, Griffiths JS, Merkel AB, Cheriyan M, Wymer NJ, Hutchins MJ, Fierke CA, Toone EJ, Naismith JH, Bioorg Med Chem. 2006 May 1;14(9):3002-10. Epub 2006 Jan 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16403639 16403639] | Mechanism of the Class I KDPG aldolase., Fullerton SW, Griffiths JS, Merkel AB, Cheriyan M, Wymer NJ, Hutchins MJ, Fierke CA, Toone EJ, Naismith JH, Bioorg Med Chem. 2006 May 1;14(9):3002-10. Epub 2006 Jan 5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16403639 16403639] | ||
| + | [[Category: 2-dehydro-3-deoxy-phosphogluconate aldolase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:13:07 2007'' |
Revision as of 10:08, 30 October 2007
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CRYSTAL STRUCTURE OF THE E45N MUTANT FROM KDPG ALDOLASE FROM ESCHERICHIA COLI
Overview
In vivo, 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase catalyzes the, reversible, stereospecific retro-aldol cleavage of KDPG to pyruvate and, D-glyceraldehyde-3-phosphate. The enzyme is a lysine-dependent (Class I), aldolase that functions through the intermediacy of a Schiff base. Here, we propose a mechanism for this enzyme based on crystallographic studies, of wild-type and mutant aldolases. The three dimensional structure of KDPG, aldolase from the thermophile Thermotoga maritima was determined to 1.9A., The structure is the standard alpha/beta barrel observed for all Class I, aldolases. At the active site Lys we observe clear density for a pyruvate, Schiff base. Density for a sulfate ion bound in a conserved cluster of, residues close to the Schiff base is also observed. We have ... [(full description)]
About this Structure
1WBH is a [Single protein] structure of sequence from [Escherichia coli] with PO4 as [ligand]. Active as [2-dehydro-3-deoxy-phosphogluconate aldolase], with EC number [4.1.2.14]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Mechanism of the Class I KDPG aldolase., Fullerton SW, Griffiths JS, Merkel AB, Cheriyan M, Wymer NJ, Hutchins MJ, Fierke CA, Toone EJ, Naismith JH, Bioorg Med Chem. 2006 May 1;14(9):3002-10. Epub 2006 Jan 5. PMID:16403639
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