1hp1: Difference between revisions

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[[Image:1hp1.gif|left|200px]]<br /><applet load="1hp1" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1hp1.gif|left|200px]]<br /><applet load="1hp1" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1hp1, resolution 1.70Å" />

'''5'-NUCLEOTIDASE (OPEN FORM) COMPLEX WITH ATP'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1HP1 OCA].

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==

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[[Category: metallophosphatase]]

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@@ Line 1: / Line 1: @@
-[[Image:1hp1.gif|left|200px]]<br /><applet load="1hp1" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1hp1.gif|left|200px]]<br /><applet load="1hp1" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1hp1, resolution 1.70&Aring;" />
 '''5'-NUCLEOTIDASE (OPEN FORM) COMPLEX WITH ATP'''<br />
 ==Overview==
-'-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.
+'-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==
-HP1 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HP1 OCA].
+HP1 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==
@@ Line 25: / Line 25: @@
 [[Category: metallophosphatase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:43:09 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:28 2008''