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2bpl

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{{STRUCTURE_2bpl| PDB=2bpl | SCENE= }}
{{STRUCTURE_2bpl| PDB=2bpl | SCENE= }}
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'''E.COLI GLUCOSAMINE-6P SYNTHASE IN COMPLEX WITH FRUCTOSE-6P'''
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===E.COLI GLUCOSAMINE-6P SYNTHASE IN COMPLEX WITH FRUCTOSE-6P===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16339762 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16339762}}
==About this Structure==
==About this Structure==
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[[Category: N terminal nucleophile]]
[[Category: N terminal nucleophile]]
[[Category: Transferase]]
[[Category: Transferase]]
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Revision as of 05:42, 28 July 2008

Template:STRUCTURE 2bpl

E.COLI GLUCOSAMINE-6P SYNTHASE IN COMPLEX WITH FRUCTOSE-6P

Template:ABSTRACT PUBMED 16339762

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

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