1zwj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zwj.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1zwj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zwj| PDB=1zwj | SCENE= }}
{{STRUCTURE_1zwj| PDB=1zwj | SCENE= }}
-
'''X-ray structure of galt-like protein from arabidopsis thaliana AT5G18200'''
+
===X-ray structure of galt-like protein from arabidopsis thaliana AT5G18200===
-
==Overview==
+
<!--
-
The X-ray crystal structure of the At5g18200.1 protein has been determined to a nominal resolution of 2.30 A. The structure has a histidine triad (HIT)-like fold containing two distinct HIT-like motifs. The sequence of At5g18200.1 indicates a distant family relationship to the Escherichia coli galactose-1-P uridylyltransferase (GalT): the determined structure of the At5g18200.1 protein confirms this relationship. The At5g18200.1 protein does not demonstrate GalT activity but instead catalyzes adenylyl transfer in the reaction of ADP-glucose with various phosphates. The best acceptor among those evaluated is phosphate itself; thus, the At5g18200.1 enzyme appears to be an ADP-glucose phosphorylase. The enzyme catalyzes the exchange of (14)C between ADP-[(14)C]glucose and glucose-1-P in the absence of phosphate. The steady state kinetics of exchange follows the ping-pong bi-bi kinetic mechanism, with a k(cat) of 4.1 s(-)(1) and K(m) values of 1.4 and 83 microM for ADP-[(14)C]glucose and glucose-1-P, respectively, at pH 8.5 and 25 degrees C. The overall reaction of ADP-glucose with phosphate to produce ADP and glucose-1-P follows ping-pong bi-bi steady state kinetics, with a k(cat) of 2.7 s(-)(1) and K(m) values of 6.9 and 90 microM for ADP-glucose and phosphate, respectively, at pH 8.5 and 25 degrees C. The kinetics are consistent with a double-displacement mechanism that involves a covalent adenylyl-enzyme intermediate. The X-ray crystal structure of this intermediate was determined to 1.83 A resolution and shows the AMP group bonded to His(186). The value of K(eq) in the direction of ADP and glucose-1-P formation is 5.0 at pH 7.0 and 25 degrees C in the absence of a divalent metal ion, and it is 40 in the presence of 1 mM MgCl(2).
+
The line below this paragraph, {{ABSTRACT_PUBMED_16519510}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16519510 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16519510}}
==About this Structure==
==About this Structure==
Line 40: Line 44:
[[Category: Unknown function]]
[[Category: Unknown function]]
[[Category: Zinc]]
[[Category: Zinc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:09:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:35:28 2008''

Revision as of 07:35, 28 July 2008

Image:1zwj.png

Template:STRUCTURE 1zwj

X-ray structure of galt-like protein from arabidopsis thaliana AT5G18200

Template:ABSTRACT PUBMED 16519510

About this Structure

1ZWJ is a Single protein structure of sequence from Arabidopsis thaliana. This structure supersedes the now removed PDB entry 1vkv. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of an ADP-glucose phosphorylase from Arabidopsis thaliana., McCoy JG, Arabshahi A, Bitto E, Bingman CA, Ruzicka FJ, Frey PA, Phillips GN Jr, Biochemistry. 2006 Mar 14;45(10):3154-62. PMID:16519510

Page seeded by OCA on Mon Jul 28 10:35:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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