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1jxa

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[[Image:1jxa.gif|left|200px]]
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{{STRUCTURE_1jxa| PDB=1jxa | SCENE= }}
{{STRUCTURE_1jxa| PDB=1jxa | SCENE= }}
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'''GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE'''
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===GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE===
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==Overview==
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Glucosamine-6-phosphate synthase catalyses the first and rate-limiting step in hexosamine metabolism, converting fructose 6-phosphate into glucosamine 6-phosphate in the presence of glutamine. The crystal structure of the Escherichia coli enzyme reveals the domain organisation of the homodimeric molecule. The 18 A hydrophobic channel sequestered from the solvent connects the glutaminase and isomerase active sites, and provides a means of ammonia transfer from glutamine to sugar phosphate. The C-terminal decapeptide sandwiched between the two domains plays a central role in the transfer. Based on the structure, a mechanism of enzyme action and self-regulation is proposed. It involves large domain movements triggered by substrate binding that lead to the formation of the channel.
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(as it appears on PubMed at http://www.pubmed.gov), where 11700065 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11700065}}
==About this Structure==
==About this Structure==
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[[Category: Gene duplication]]
[[Category: Gene duplication]]
[[Category: Nucleotide-binding fold]]
[[Category: Nucleotide-binding fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:02:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:24:25 2008''

Revision as of 05:24, 29 July 2008

Image:1jxa.png

Template:STRUCTURE 1jxa

GLUCOSAMINE 6-PHOSPHATE SYNTHASE WITH GLUCOSE 6-PHOSPHATE

Template:ABSTRACT PUBMED 11700065

About this Structure

1JXA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Channeling of ammonia in glucosamine-6-phosphate synthase., Teplyakov A, Obmolova G, Badet B, Badet-Denisot MA, J Mol Biol. 2001 Nov 9;313(5):1093-102. PMID:11700065

Page seeded by OCA on Tue Jul 29 08:24:25 2008

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