1nht
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1nht |SIZE=350|CAPTION= <scene name='initialview01'>1nht</scene>, resolution 2.5Å | |PDB= 1nht |SIZE=350|CAPTION= <scene name='initialview01'>1nht</scene>, resolution 2.5Å | ||
|SITE= <scene name='pdbsite=ASP:These+Residues+Make+Up+The+Guanine+Nucleotide+Binding+Si+...'>ASP</scene>, <scene name='pdbsite=GNS:These+Residues+Make+Up+The+Guanine+Nucleotide+Binding+Si+...'>GNS</scene> and <scene name='pdbsite=IMP:These+Residues+Make+Up+The+Guanine+Nucleotide+Binding+Si+...'>IMP</scene> | |SITE= <scene name='pdbsite=ASP:These+Residues+Make+Up+The+Guanine+Nucleotide+Binding+Si+...'>ASP</scene>, <scene name='pdbsite=GNS:These+Residues+Make+Up+The+Guanine+Nucleotide+Binding+Si+...'>GNS</scene> and <scene name='pdbsite=IMP:These+Residues+Make+Up+The+Guanine+Nucleotide+Binding+Si+...'>IMP</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5 | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=HAD:(CARBOXYHYDROXYAMINO)ETHANOIC+ACID'>HAD</scene> and <scene name='pdbligand=PGS:2-DEAZO-6-THIOPHOSPHATE GUANOSINE-5'-MONOPHOSPHATE'>PGS</scene> |
|ACTIVITY= [http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4] | |ACTIVITY= [http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4] | ||
|GENE= | |GENE= | ||
| Line 37: | Line 37: | ||
[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:54:20 2008'' |
Revision as of 10:54, 23 March 2008
| |||||||
| , resolution 2.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , , and | ||||||
| Activity: | Adenylosuccinate synthase, with EC number 6.3.4.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ENTRAPMENT OF 6-THIOPHOSPHORYL-IMP IN THE ACTIVE SITE OF CRYSTALLINE ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI DATA COLLECTED AT 100K
Overview
Crystal structures of adenylosuccinate synthetase from Escherichia coli complexed with Mg2+, 6-thiophosphoryl-IMP, GDP, and hadacidin at 298 and 100 K have been refined to R-factors of 0.171 and 0.206 against data to 2.8 and 2.5 A resolution, respectively. Interactions of GDP, Mg2+ and hadacidin are similar to those observed for the same ligands in the complex of IMP, GDP, NO3-, Mg2+ and hadacidin (Poland, B. W., Fromm, H. J. & Honzatko, R. B. (1996). J. Mol. Biol. 264, 1013-1027). Although crystals were grown from solutions containing 6-mercapto-IMP and GTP, the electron density at the active site is consistent with 6-thiophosphoryl-IMP and GDP. Asp-13 and Gln-224 probably work in concert to stabilize the 6-thioanion of 6-mercapto-IMP, which in turn is the nucleophile in the displacement of GDP from the gamma-phosphate of GTP. Once formed, 6-thiophosphoryl-IMP is stable in the active site of the enzyme under the conditions of the structural investigation. The direct observation of 6-thiophosphoryl-IMP in the active site is consistent with the putative generation of 6-phosphoryl-IMP along the reaction pathway of the synthetase.
About this Structure
1NHT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Entrapment of 6-thiophosphoryl-IMP in the active site of crystalline adenylosuccinate synthetase from Escherichia coli., Poland BW, Bruns C, Fromm HJ, Honzatko RB, J Biol Chem. 1997 Jun 13;272(24):15200-5. PMID:9182542
Page seeded by OCA on Sun Mar 23 12:54:20 2008
