2bpl
From Proteopedia
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|PDB= 2bpl |SIZE=350|CAPTION= <scene name='initialview01'>2bpl</scene>, resolution 2.05Å | |PDB= 2bpl |SIZE=350|CAPTION= <scene name='initialview01'>2bpl</scene>, resolution 2.05Å | ||
|SITE= <scene name='pdbsite=AC1:F6r+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:F6r+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=F6R:FRUCTOSE -6-PHOSPHATE'>F6R</scene> | + | |LIGAND= <scene name='pdbligand=F6R:FRUCTOSE+-6-PHOSPHATE'>F6R</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2bpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bpl OCA], [http://www.ebi.ac.uk/pdbsum/2bpl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2bpl RCSB]</span> | ||
}} | }} | ||
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[[Category: Golinelli-Pimpaneau, B.]] | [[Category: Golinelli-Pimpaneau, B.]] | ||
[[Category: Mouilleron, S.]] | [[Category: Mouilleron, S.]] | ||
| - | [[Category: F6R]] | ||
[[Category: amidotransferase]] | [[Category: amidotransferase]] | ||
[[Category: ammonia channeling]] | [[Category: ammonia channeling]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:09:51 2008'' |
Revision as of 23:09, 30 March 2008
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| , resolution 2.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Glutamine--fructose-6-phosphate transaminase (isomerizing), with EC number 2.6.1.16 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
E.COLI GLUCOSAMINE-6P SYNTHASE IN COMPLEX WITH FRUCTOSE-6P
Overview
Glucosamine-6P synthase catalyzes the synthesis of glucosamine-6P from fructose-6P and glutamine and uses a channel to transfer ammonia from its glutaminase to its synthase active site. X-ray structures of glucosamine-6P synthase have been determined at 2.05 Angstroms resolution in the presence of fructose-6P and at 2.35 Angstroms resolution in the presence of fructose-6P and 6-diazo-5-oxo-L-norleucine, a glutamine affinity analog that covalently modifies the N-terminal catalytic cysteine, therefore mimicking the gamma-glutamyl-thioester intermediate formed during hydrolysis of glutamine. The fixation of the glutamine analog activates the enzyme through several major structural changes: 1) the closure of a loop to shield the glutaminase site accompanied by significant domain hinging, 2) the activation of catalytic residues involved in glutamine hydrolysis, i.e. the alpha-amino group of Cys-1 and Asn-98 that is positioned to form the oxyanion hole, and 3) a 75 degrees rotation of the Trp-74 indole group that opens the ammonia channel.
About this Structure
2BPL is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Glutamine binding opens the ammonia channel and activates glucosamine-6P synthase., Mouilleron S, Badet-Denisot MA, Golinelli-Pimpaneau B, J Biol Chem. 2006 Feb 17;281(7):4404-12. Epub 2005 Dec 9. PMID:16339762
Page seeded by OCA on Mon Mar 31 02:09:51 2008
Categories: Escherichia coli | Glutamine--fructose-6-phosphate transaminase (isomerizing) | Single protein | Golinelli-Pimpaneau, B. | Mouilleron, S. | Amidotransferase | Ammonia channeling | Fructose 6-phosphate | Glucosamine 6-phosphate synthase | Glutamine amidotransferase | N terminal nucleophile | Transferase
