1hor: Difference between revisions
New page: left|200px<br /><applet load="1hor" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hor, resolution 2.4Å" /> '''STRUCTURE AND CATALYT... |
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[[Image:1hor.gif|left|200px]]<br /><applet load="1hor" size=" | [[Image:1hor.gif|left|200px]]<br /><applet load="1hor" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1hor, resolution 2.4Å" /> | caption="1hor, resolution 2.4Å" /> | ||
'''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 | 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== | ||
1HOR 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 and AGP as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | 1HOR 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> and <scene name='pdbligand=AGP:'>AGP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=1HOR 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 | [[Category: Altamirano, M M.]] | ||
[[Category: Calcagno, M | [[Category: Calcagno, M L.]] | ||
[[Category: Fontes, M | [[Category: Fontes, M R.M.]] | ||
[[Category: Garratt, R | [[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]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:19 2008'' |