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| - | [[Image:1z84.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1z84| PDB=1z84 | SCENE= }} | | {{STRUCTURE_1z84| PDB=1z84 | SCENE= }} |
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| - | '''X-ray structure of galt-like protein from arabidopsis thaliana at5g18200'''
| + | ===X-ray structure of galt-like protein from arabidopsis thaliana at5g18200=== |
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| - | ==Overview==
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| - | 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. |
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| | + | {{ABSTRACT_PUBMED_16519510}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| | [[Category: Zinc]] | | [[Category: Zinc]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:17:45 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:11:20 2008'' |
Revision as of 10:11, 28 July 2008
Template:STRUCTURE 1z84
X-ray structure of galt-like protein from arabidopsis thaliana at5g18200
Template:ABSTRACT PUBMED 16519510
About this Structure
1Z84 is a Single protein structure of sequence from Arabidopsis thaliana. 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 13:11:20 2008
