1hp1
From Proteopedia
(New page: 200px<br /><applet load="1hp1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hp1, resolution 1.70Å" /> '''5'-NUCLEOTIDASE (OPE...) |
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| - | [[Image:1hp1.gif|left|200px]]<br /><applet load="1hp1" size=" | + | [[Image:1hp1.gif|left|200px]]<br /><applet load="1hp1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hp1, resolution 1.70Å" /> | caption="1hp1, resolution 1.70Å" /> | ||
'''5'-NUCLEOTIDASE (OPEN FORM) COMPLEX WITH ATP'''<br /> | '''5'-NUCLEOTIDASE (OPEN FORM) COMPLEX WITH ATP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | 5'-Nucleotidase belongs to a large superfamily of distantly related | + | 5'-Nucleotidase belongs to a large superfamily of distantly related dinuclear metallophosphatases including the Ser/Thr protein phosphatases and purple acid phosphatases. The protein undergoes a 96 degrees domain rotation between an open (inactive) and a closed (active) enzyme form. Complex structures of the closed form with the products adenosine and phosphate, and with the substrate analogue inhibitor alpha,beta-methylene ADP, have been determined at 2.1 A and 1.85 A resolution, respectively. In addition, a complex of the open form of 5'-nucleotidase with ATP was analyzed at a resolution of 1.7 A. These structures show that the adenosine group binds to a specific binding pocket of the C-terminal domain. The adenine ring is stacked between Phe429 and Phe498. The N-terminal domain provides the ligands to the dimetal cluster and the conserved His117, which together form the catalytic core structure. However, the three C-terminal arginine residues 375, 379 and 410, which are involved in substrate binding, may also play a role in transition-state stabilization. The beta-phosphate group of the inhibitor is terminally coordinated to the site 2 metal ion. The site 1 metal ion coordinates a water molecule which is in an ideal position for a nucleophilic attack on the phosphorus atom, assuming an in-line mechanism of phosphoryl transfer. Another water molecule bridges the two metal ions. |
==About this Structure== | ==About this Structure== | ||
| - | 1HP1 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 ZN, CO3, SO4 and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1HP1 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=ZN:'>ZN</scene>, <scene name='pdbligand=CO3:'>CO3</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HP1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: metallophosphatase]] | [[Category: metallophosphatase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:28 2008'' |
Revision as of 11:03, 21 February 2008
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5'-NUCLEOTIDASE (OPEN FORM) COMPLEX WITH ATP
Overview
5'-Nucleotidase belongs to a large superfamily of distantly related dinuclear metallophosphatases including the Ser/Thr protein phosphatases and purple acid phosphatases. The protein undergoes a 96 degrees domain rotation between an open (inactive) and a closed (active) enzyme form. Complex structures of the closed form with the products adenosine and phosphate, and with the substrate analogue inhibitor alpha,beta-methylene ADP, have been determined at 2.1 A and 1.85 A resolution, respectively. In addition, a complex of the open form of 5'-nucleotidase with ATP was analyzed at a resolution of 1.7 A. These structures show that the adenosine group binds to a specific binding pocket of the C-terminal domain. The adenine ring is stacked between Phe429 and Phe498. The N-terminal domain provides the ligands to the dimetal cluster and the conserved His117, which together form the catalytic core structure. However, the three C-terminal arginine residues 375, 379 and 410, which are involved in substrate binding, may also play a role in transition-state stabilization. The beta-phosphate group of the inhibitor is terminally coordinated to the site 2 metal ion. The site 1 metal ion coordinates a water molecule which is in an ideal position for a nucleophilic attack on the phosphorus atom, assuming an in-line mechanism of phosphoryl transfer. Another water molecule bridges the two metal ions.
About this Structure
1HP1 is a Single protein structure of sequence from Escherichia coli with , , and as ligands. Full crystallographic information is available from OCA.
Reference
Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures., Knofel T, Strater N, J Mol Biol. 2001 May 25;309(1):239-54. PMID:11491293
Page seeded by OCA on Thu Feb 21 13:03:28 2008
Categories: Escherichia coli | Single protein | Knoefel, T. | Straeter, N. | ATP | CO3 | SO4 | ZN | Dinuclear | Domain movement | Hydrolase | Metalloenzyme | Metallophosphatase
