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| - | [[Image:1hp1.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1hp1.png|left|200px]] |
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| | {{STRUCTURE_1hp1| PDB=1hp1 | SCENE= }} | | {{STRUCTURE_1hp1| PDB=1hp1 | SCENE= }} |
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| - | '''5'-NUCLEOTIDASE (OPEN FORM) COMPLEX WITH ATP'''
| + | ===5'-NUCLEOTIDASE (OPEN FORM) COMPLEX WITH ATP=== |
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| - | ==Overview==
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| - | 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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11491293}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11491293 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11491293}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Metalloenzyme]] | | [[Category: Metalloenzyme]] |
| | [[Category: Metallophosphatase]] | | [[Category: Metallophosphatase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:04:57 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:29:17 2008'' |
Revision as of 05:29, 1 July 2008
Template:STRUCTURE 1hp1
5'-NUCLEOTIDASE (OPEN FORM) COMPLEX WITH ATP
Template:ABSTRACT PUBMED 11491293
About this Structure
1HP1 is a Single protein structure of sequence from Escherichia coli. 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 Tue Jul 1 08:29:17 2008
