1hpu
From Proteopedia
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|PDB= 1hpu |SIZE=350|CAPTION= <scene name='initialview01'>1hpu</scene>, resolution 1.85Å | |PDB= 1hpu |SIZE=350|CAPTION= <scene name='initialview01'>1hpu</scene>, resolution 1.85Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=A12:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENOSYL+ESTER'>A12</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= USHA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= USHA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ush|1USH]], [[2ush|2USH]], [[1hp1|1HP1]], [[1ho5|1HO5]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hpu OCA], [http://www.ebi.ac.uk/pdbsum/1hpu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hpu RCSB]</span> | ||
}} | }} | ||
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[[Category: Knoefel, T.]] | [[Category: Knoefel, T.]] | ||
[[Category: Straeter, N.]] | [[Category: Straeter, N.]] | ||
| - | [[Category: A12]] | ||
| - | [[Category: MN]] | ||
[[Category: domain movement]] | [[Category: domain movement]] | ||
[[Category: domain rotation]] | [[Category: domain rotation]] | ||
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[[Category: metallophosphatase]] | [[Category: metallophosphatase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:08:48 2008'' |
Revision as of 18:08, 30 March 2008
| |||||||
| , resolution 1.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | USHA (Escherichia coli) | ||||||
| Related: | 1USH, 2USH, 1HP1, 1HO5
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
5'-NUCLEOTIDASE (CLOSED FORM), COMPLEX WITH AMPCP
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
1HPU 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
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