1hpu: Difference between revisions
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[[Image:1hpu.gif|left|200px]] | [[Image:1hpu.gif|left|200px]] | ||
'''5'-NUCLEOTIDASE (CLOSED FORM), COMPLEX WITH AMPCP''' | {{Structure | ||
|PDB= 1hpu |SIZE=350|CAPTION= <scene name='initialview01'>1hpu</scene>, resolution 1.85Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=A12:PHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER'>A12</scene> | |||
|ACTIVITY= | |||
|GENE= USHA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''5'-NUCLEOTIDASE (CLOSED FORM), COMPLEX WITH AMPCP''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1HPU is a [ | 1HPU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HPU OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11491293 11491293] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: metallophosphatase]] | [[Category: metallophosphatase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:40:03 2008'' | ||
Revision as of 12:40, 20 March 2008
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| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | USHA (Escherichia coli) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
5'-NUCLEOTIDASE (CLOSED FORM), COMPLEX WITH AMPCP
OverviewOverview
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 StructureAbout this Structure
1HPU is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
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
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