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1moq
From Proteopedia
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|PDB= 1moq |SIZE=350|CAPTION= <scene name='initialview01'>1moq</scene>, resolution 1.57Å | |PDB= 1moq |SIZE=350|CAPTION= <scene name='initialview01'>1moq</scene>, resolution 1.57Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=GLP:GLUCOSAMINE+6-PHOSPHATE'>GLP</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GLP:GLUCOSAMINE+6-PHOSPHATE'>GLP</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</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=1moq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1moq OCA], [http://www.ebi.ac.uk/pdbsum/1moq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1moq RCSB]</span> | ||
}} | }} | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Teplyakov, A.]] | [[Category: Teplyakov, A.]] | ||
| - | [[Category: GLP]] | ||
| - | [[Category: MES]] | ||
| - | [[Category: MRD]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: SO4]] | ||
[[Category: glutamine amidotransferase]] | [[Category: glutamine amidotransferase]] | ||
| - | ''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 22:19:01 2008'' |
Revision as of 19:19, 30 March 2008
| |||||||
| , resolution 1.57Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 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
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