This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1hor

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hor.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1hor.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1hor| PDB=1hor | SCENE= }}
{{STRUCTURE_1hor| PDB=1hor | SCENE= }}
-
'''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===
-
==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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8747459}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8747459 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8747459}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[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 19:04:24 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:28:37 2008''

Revision as of 05:28, 1 July 2008

Image:1hor.png

Template:STRUCTURE 1hor

STRUCTURE AND CATALYTIC MECHANISM OF GLUCOSAMINE 6-PHOSPHATE DEAMINASE FROM ESCHERICHIA COLI AT 2.1 ANGSTROMS RESOLUTION

Template:ABSTRACT PUBMED 8747459

About this Structure

1HOR 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 Tue Jul 1 08:28:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hor"
Personal tools