1mos: Difference between revisions

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[[Image:1mos.gif|left|200px]]
{{Seed}}
[[Image:1mos.png|left|200px]]


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{{STRUCTURE_1mos|  PDB=1mos  |  SCENE=  }}  
{{STRUCTURE_1mos|  PDB=1mos  |  SCENE=  }}  


'''ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH 2-AMINO-2-DEOXYGLUCITOL 6-PHOSPHATE'''
===ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH 2-AMINO-2-DEOXYGLUCITOL 6-PHOSPHATE===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_10091662}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 10091662 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10091662}}


==About this Structure==
==About this Structure==
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[[Category: Glutamine amidotransferase]]
[[Category: Glutamine amidotransferase]]
[[Category: Transferase]]
[[Category: Transferase]]
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