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2cgl
From Proteopedia
(New page: 200px<br /> <applet load="2cgl" size="450" color="white" frame="true" align="right" spinBox="true" caption="2cgl, resolution 1.88Å" /> '''CRYSTAL STRUCTURE O...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2CGL 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 LFR and ADP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.5 2.7.1.5]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CGL OCA]]. | + | 2CGL 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 LFR and ADP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Rhamnulokinase Rhamnulokinase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.5 2.7.1.5]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CGL OCA]]. |
==Reference== | ==Reference== | ||
Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli., Grueninger D, Schulz GE, J Mol Biol. 2006 Jun 9;359(3):787-97. Epub 2006 Apr 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16674975 16674975] | Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli., Grueninger D, Schulz GE, J Mol Biol. 2006 Jun 9;359(3):787-97. Epub 2006 Apr 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16674975 16674975] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Rhamnulokinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Grueninger, D.]] | [[Category: Grueninger, D.]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''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 14:18:21 2007'' |
Revision as of 12:13, 30 October 2007
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CRYSTAL STRUCTURE OF L-RHAMNULOSE KINASE FROM ESCHERICHIA COLI IN COMPLEX WITH L-FRUCTOSE, ADP AND A MODELED ATP GAMMA PHOSPHATE.
Overview
Bacterial L-rhamnulose kinase participates in the degradation of, L-rhamnose, which is ubiquitous and particularly abundant in some plants., The enzyme catalyzes the transfer of the gamma-phosphate group from ATP to, the 1-hydroxyl group of L-rhamnulose. We determined the crystal structures, of the substrate-free kinase and of a complex between the enzyme, ADP and, L-fructose, which besides rhamnulose is also processed. According to its, chainfold, the kinase belongs to the hexokinase-hsp70-actin superfamily., The closest structurally known homologue is glycerol kinase. The reported, structures reveal a large conformational change on substrate binding as, well as the key residues involved in catalysis. The substrates ADP and, beta-L-fructose are in an ideal position to define a direct ... [(full description)]
About this Structure
2CGL is a [Single protein] structure of sequence from [Escherichia coli] with LFR and ADP as [ligands]. Active as [Rhamnulokinase], with EC number [2.7.1.5]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structure and reaction mechanism of L-rhamnulose kinase from Escherichia coli., Grueninger D, Schulz GE, J Mol Biol. 2006 Jun 9;359(3):787-97. Epub 2006 Apr 25. PMID:16674975
Page seeded by OCA on Tue Oct 30 14:18:21 2007
