1qm5
From Proteopedia
(New page: 200px<br /> <applet load="1qm5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qm5, resolution 2.0Å" /> '''PHOSPHORYLASE RECOGN...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1QM5 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 GLC, PO4 and PLP 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=2.4.1.1 2.4.1.1]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QM5 OCA]]. | + | 1QM5 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 GLC, PO4 and PLP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1]]. Structure known Active Sites: CAA and CAB. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QM5 OCA]]. |
==Reference== | ==Reference== | ||
Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question., Watson KA, McCleverty C, Geremia S, Cottaz S, Driguez H, Johnson LN, EMBO J. 1999 Sep 1;18(17):4619-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10469642 10469642] | Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question., Watson KA, McCleverty C, Geremia S, Cottaz S, Driguez H, Johnson LN, EMBO J. 1999 Sep 1;18(17):4619-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10469642 10469642] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Phosphorylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cottaz, S.]] | [[Category: Cottaz, S.]] | ||
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[[Category: thio-oligosaccharide]] | [[Category: thio-oligosaccharide]] | ||
| - | ''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 14:27:39 2007'' |
Revision as of 12:22, 30 October 2007
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PHOSPHORYLASE RECOGNITION AND PHOSPHORYLYSIS OF ITS OLIGOSACCHARIDE SUBSTRATE: ANSWERS TO A LONG OUTSTANDING QUESTION
Overview
Phosphorylases are key enzymes of carbohydrate metabolism. Structural, studies have provided explanations for almost all features of control and, substrate recognition of phosphorylase but one question remains, unanswered. How does phosphorylase recognize and cleave an oligosaccharide, substrate? To answer this question we turned to the Escherichia coli, maltodextrin phosphorylase (MalP), a non-regulatory phosphorylase that, shares similar kinetic and catalytic properties with the mammalian, glycogen phosphorylase. The crystal structures of three, MalP-oligosaccharide complexes are reported: the binary complex of MalP, with the natural substrate, maltopentaose (G5); the binary complex with, the thio-oligosaccharide, 4-S-alpha-D-glucopyranosyl-4-thiomaltotetraose, (GSG4), both at 2.9 A ... [(full description)]
About this Structure
1QM5 is a [Single protein] structure of sequence from [Escherichia coli] with GLC, PO4 and PLP as [ligands]. Active as [Phosphorylase], with EC number [2.4.1.1]. Structure known Active Sites: CAA and CAB. Full crystallographic information is available from [OCA].
Reference
Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question., Watson KA, McCleverty C, Geremia S, Cottaz S, Driguez H, Johnson LN, EMBO J. 1999 Sep 1;18(17):4619-32. PMID:10469642
Page seeded by OCA on Tue Oct 30 14:27:39 2007
