1dea
From Proteopedia
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| - | [[Image:1dea.jpg|left|200px]] | + | [[Image:1dea.jpg|left|200px]] |
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| - | '''STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION''' | + | {{Structure |
| + | |PDB= 1dea |SIZE=350|CAPTION= <scene name='initialview01'>1dea</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=PO4:PHOSPHATE ION'>PO4</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Glucosamine-6-phosphate_deaminase Glucosamine-6-phosphate deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.99.6 3.5.99.6] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DEA is a [ | + | 1DEA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEA OCA]. |
==Reference== | ==Reference== | ||
| - | Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution., Oliva G, Fontes MR, Garratt RC, Altamirano MM, Calcagno ML, Horjales E, Structure. 1995 Dec 15;3(12):1323-32. PMID:[http:// | + | Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution., Oliva G, Fontes MR, Garratt RC, Altamirano MM, Calcagno ML, Horjales E, Structure. 1995 Dec 15;3(12):1323-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8747459 8747459] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Glucosamine-6-phosphate deaminase]] | [[Category: Glucosamine-6-phosphate deaminase]] | ||
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[[Category: intramolecular oxidoreductase deaminase]] | [[Category: intramolecular oxidoreductase deaminase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:37:07 2008'' |
Revision as of 08:37, 20 March 2008
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| , resolution 2.1Å | |||||||
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| Ligands: | |||||||
| Activity: | Glucosamine-6-phosphate deaminase, with EC number 3.5.99.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION
Overview
BACKGROUND: Glucosamine 6-phosphate deaminase from Escherichia coli is an allosteric hexameric enzyme which catalyzes the reversible conversion of D-glucosamine 6-phosphate into D-fructose 6-phosphate and ammonium ion and is activated by N-acetyl-D-glucosamine 6-phosphate. Mechanistically, it belongs to the group of aldoseketose isomerases, but its reaction also accomplishes a simultaneous amination/deamination. The determination of the structure of this protein provides fundamental knowledge for understanding its mode of action and the nature of allosteric conformational changes that regulate its function. RESULTS: The crystal structure of glucosamine 6-phosphate deaminase with bound phosphate ions is presented at 2.1 A resolution together with the refined structures of the enzyme in complexes with its allosteric activator and with a competitive inhibitor. The protein fold can be described as a modified NAD-binding domain. CONCLUSIONS: From the similarities between the three presented structures, it is concluded that these represent the enzymatically active R state conformer. A mechanism for the deaminase reaction is proposed. It comprises steps to open the pyranose ring of the substrate and a sequence of general base-catalyzed reactions to bring about isomerization and deamination, with Asp72 playing a key role as a proton exchanger.
About this Structure
1DEA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution., Oliva G, Fontes MR, Garratt RC, Altamirano MM, Calcagno ML, Horjales E, Structure. 1995 Dec 15;3(12):1323-32. PMID:8747459
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