1moq
From Proteopedia
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'''ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSAMINE 6-PHOSPHATE''' | '''ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSAMINE 6-PHOSPHATE''' | ||
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Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain., Teplyakov A, Obmolova G, Badet-Denisot MA, Badet B, Polikarpov I, Structure. 1998 Aug 15;6(8):1047-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9739095 9739095] | Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain., Teplyakov A, Obmolova G, Badet-Denisot MA, Badet B, Polikarpov I, Structure. 1998 Aug 15;6(8):1047-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9739095 9739095] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Glutamine--fructose-6-phosphate transaminase (isomerizing)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Teplyakov, A.]] | [[Category: Teplyakov, A.]] | ||
| - | [[Category: | + | [[Category: Glutamine amidotransferase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:31:48 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 22:31, 2 May 2008
ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSAMINE 6-PHOSPHATE
Overview
BACKGROUND: Glucosamine 6-phosphate synthase (GlmS) catalyses the first step in hexosamine metabolism, converting fructose-6P (6 phosphate) into glucosamine-6P using glutamine as a nitrogen source. GlmS is a bienzyme complex consisting of two domains that catalyse glutamine hydrolysis and sugar-phosphate isomerisation, respectively. Knowledge of the three-dimensional structure of GlmS is essential for understanding the general principles of catalysis by ketol isomerases and the mechanism of nitrogen transfer in glutamine amidotransferases. RESULTS: The crystal structure of the isomerase domain of the Escherichia coli GlmS with the reaction product, glucosamine-6P, has been determined at 1.57 A resolution. It is comprised of two topologically identical subdomains, each of which is dominated by a nucleotide-binding motif of a flavodoxin type. The catalytic site is assembled by dimerisation of the protein. CONCLUSIONS: The isomerase active site of GlmS seems to be the result of evolution through gene duplication and subsequent dimerisation. Isomerisation of fructose-6P is likely to involve the formation of a Schiff base with Lys603 of the enzyme, the ring-opening step catalysed by His504, and the proton transfer from C1 to C2 of the substrate effected by Glu488. The highly conserved C-terminal fragment of the chain may play a key role in substrate binding, catalysis and communication with the glutaminase domain. The corresponding sequence pattern DXPXXLAK[SC]VT (in single-letter amino-acid code, where X is any amino acid and letters in brackets indicate that either serine or cysteine may take this position) may be considered as a fingerprint of GlmS.
About this Structure
1MOQ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain., Teplyakov A, Obmolova G, Badet-Denisot MA, Badet B, Polikarpov I, Structure. 1998 Aug 15;6(8):1047-55. PMID:9739095 Page seeded by OCA on Sat May 3 01:31:48 2008
