1dea

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1dea.jpg|left|200px]]
[[Image:1dea.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1dea |SIZE=350|CAPTION= <scene name='initialview01'>1dea</scene>, resolution 2.1&Aring;
+
The line below this paragraph, containing "STRUCTURE_1dea", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[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] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1dea| PDB=1dea | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dea OCA], [http://www.ebi.ac.uk/pdbsum/1dea PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dea RCSB]</span>
+
-
}}
+
'''STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION'''
'''STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION'''
Line 32: Line 29:
[[Category: Horjales, E.]]
[[Category: Horjales, E.]]
[[Category: Oliva, G.]]
[[Category: Oliva, G.]]
-
[[Category: intramolecular oxidoreductase deaminase]]
+
[[Category: Intramolecular oxidoreductase deaminase]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 13:45:17 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:39:55 2008''
+

Revision as of 10:45, 2 May 2008

Template:STRUCTURE 1dea

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 Page seeded by OCA on Fri May 2 13:45:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools