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New page: left|200px<br /><applet load="1dea" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dea, resolution 2.1Å" /> '''STRUCTURE AND CATALYT...
 
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[[Image:1dea.jpg|left|200px]]<br /><applet load="1dea" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1dea.jpg|left|200px]]<br /><applet load="1dea" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1dea, resolution 2.1&Aring;" />
caption="1dea, resolution 2.1&Aring;" />
'''STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION'''<br />
'''STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION'''<br />


==Overview==
==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.
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==
==About this Structure==
1DEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1DEA OCA].  
1DEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DEA OCA].  


==Reference==
==Reference==
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[[Category: Glucosamine-6-phosphate deaminase]]
[[Category: Glucosamine-6-phosphate deaminase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Altamirano, M.M.]]
[[Category: Altamirano, M M.]]
[[Category: Calcagno, M.L.]]
[[Category: Calcagno, M L.]]
[[Category: Fontes, M.R.M.]]
[[Category: Fontes, M R.M.]]
[[Category: Garratt, R.C.]]
[[Category: Garratt, R C.]]
[[Category: Horjales, E.]]
[[Category: Horjales, E.]]
[[Category: Oliva, G.]]
[[Category: Oliva, G.]]
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[[Category: intramolecular oxidoreductase deaminase]]
[[Category: intramolecular oxidoreductase deaminase]]


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