1hp1
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1hp1 |SIZE=350|CAPTION= <scene name='initialview01'>1hp1</scene>, resolution 1.70Å | |PDB= 1hp1 |SIZE=350|CAPTION= <scene name='initialview01'>1hp1</scene>, resolution 1.70Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]], [[1ho5|1HO5]], [[1hpu|1HPU]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hp1 OCA], [http://www.ebi.ac.uk/pdbsum/1hp1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hp1 RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Knoefel, T.]] | [[Category: Knoefel, T.]] | ||
[[Category: Straeter, N.]] | [[Category: Straeter, N.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: CO3]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: dinuclear]] | [[Category: dinuclear]] | ||
[[Category: domain movement]] | [[Category: domain movement]] | ||
| Line 34: | Line 33: | ||
[[Category: metallophosphatase]] | [[Category: metallophosphatase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:08:34 2008'' |
Revision as of 18:08, 30 March 2008
| |||||||
| , resolution 1.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | USHA (Escherichia coli) | ||||||
| Related: | 1USH, 2USH, 1HO5, 1HPU
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 21:08:34 2008
