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1mos
From Proteopedia
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|PDB= 1mos |SIZE=350|CAPTION= <scene name='initialview01'>1mos</scene>, resolution 2.00Å | |PDB= 1mos |SIZE=350|CAPTION= <scene name='initialview01'>1mos</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AGP:2-DEOXY-2-AMINO+GLUCITOL-6-PHOSPHATE'>AGP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1mos FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mos OCA], [http://www.ebi.ac.uk/pdbsum/1mos PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mos RCSB]</span> | ||
}} | }} | ||
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[[Category: Obmolova, G.]] | [[Category: Obmolova, G.]] | ||
[[Category: Teplyakov, A.]] | [[Category: Teplyakov, A.]] | ||
| - | [[Category: AGP]] | ||
| - | [[Category: MES]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: SO4]] | ||
[[Category: aminotransferase]] | [[Category: aminotransferase]] | ||
[[Category: glutamine amidotransferase]] | [[Category: glutamine amidotransferase]] | ||
[[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 Sun Mar 30 22:18:59 2008'' |
Revision as of 19:19, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 | ||||||
ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH 2-AMINO-2-DEOXYGLUCITOL 6-PHOSPHATE
Overview
Glucosamine 6-phosphate synthase converts fructose-6P into glucosamine-6P or glucose-6P depending on the presence or absence of glutamine. The isomerase activity is associated with a 40-kDa C-terminal domain, which has already been characterized crystallographically. Now the three-dimensional structures of the complexes with the reaction product glucose-6P and with the transition state analog 2-amino-2-deoxyglucitol-6P have been determined. Glucose-6P binds in a cyclic form whereas 2-amino-2-deoxyglucitol-6P is in an extended conformation. The information on ligand-protein interactions observed in the crystal structures together with the isotope exchange and site-directed mutagenesis data allow us to propose a mechanism of the isomerase activity of glucosamine-6P synthase. The sugar phosphate isomerization involves a ring opening step catalyzed by His504 and an enolization step with Glu488 catalyzing the hydrogen transfer from C1 to C2 of the substrate. The enediol intermediate is stabilized by a helix dipole and the epsilon-amino group of Lys603. Lys485 may play a role in deprotonating the hydroxyl O1 of the intermediate.
About this Structure
1MOS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase., Teplyakov A, Obmolova G, Badet-Denisot MA, Badet B, Protein Sci. 1999 Mar;8(3):596-602. PMID:10091662
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