1nht
From Proteopedia
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| - | [[Image:1nht.jpg|left|200px]] | + | [[Image:1nht.jpg|left|200px]] |
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| - | '''ENTRAPMENT OF 6-THIOPHOSPHORYL-IMP IN THE ACTIVE SITE OF CRYSTALLINE ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI DATA COLLECTED AT 100K''' | + | {{Structure |
| + | |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> | ||
| + | |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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ENTRAPMENT OF 6-THIOPHOSPHORYL-IMP IN THE ACTIVE SITE OF CRYSTALLINE ADENYLOSUCCINATE SYNTHETASE FROM ESCHERICHIA COLI DATA COLLECTED AT 100K''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NHT is a [ | + | 1NHT 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=1NHT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9182542 9182542] |
[[Category: Adenylosuccinate synthase]] | [[Category: Adenylosuccinate synthase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: MG]] | [[Category: MG]] | ||
[[Category: PGS]] | [[Category: PGS]] | ||
| - | [[Category: gtp-hydrolysing | + | [[Category: gtp-hydrolysing enzyme]] |
[[Category: ligase]] | [[Category: ligase]] | ||
[[Category: purine nucleotide biosynthesis]] | [[Category: purine nucleotide biosynthesis]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''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 12:57:04 2008'' |
Revision as of 10:57, 20 March 2008
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| , resolution 2.5Å | |||||||
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| 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
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