1jdb
From Proteopedia
(New page: 200px<br /><applet load="1jdb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jdb, resolution 2.1Å" /> '''CARBAMOYL PHOSPHATE S...) |
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| - | [[Image:1jdb.gif|left|200px]]<br /><applet load="1jdb" size=" | + | [[Image:1jdb.gif|left|200px]]<br /><applet load="1jdb" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jdb, resolution 2.1Å" /> | caption="1jdb, resolution 2.1Å" /> | ||
'''CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI'''<br /> | '''CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Carbamoyl phosphate synthetase catalyzes the formation of carbamoyl | + | Carbamoyl phosphate synthetase catalyzes the formation of carbamoyl phosphate from one molecule of bicarbonate, two molecules of Mg2+ATP and one molecule of glutamine or ammonia depending upon the particular form of the enzyme under investigation. As isolated from Escherichia coli, the enzyme is an alpha,beta-heterodimer consisting of a small subunit that hydrolyzes glutamine and a large subunit that catalyzes the two required phosphorylation events. Here the three-dimensional structure of carbamoyl phosphate synthetase from E. coli refined to 2.1 A resolution with an R factor of 17.9% is described. The small subunit is distinctly bilobal with a catalytic triad (Cys269, His353 and Glu355) situated between the two structural domains. As observed in those enzymes belonging to the alpha/beta-hydrolase family, the active-site nucleophile, Cys269, is perched at the top of a tight turn. The large subunit consists of four structural units: the carboxyphosphate synthetic component, the oligomerization domain, the carbamoyl phosphate synthetic component and the allosteric domain. Both the carboxyphosphate and carbamoyl phosphate synthetic components bind Mn2+ADP. In the carboxyphosphate synthetic component, the two observed Mn2+ ions are both octahedrally coordinated by oxygen-containing ligands and are bridged by the carboxylate side chain of Glu299. Glu215 plays a key allosteric role by coordinating to the physiologically important potassium ion and hydrogen bonding to the ribose hydroxyl groups of ADP. In the carbamoyl phosphate synthetic component, the single observed Mn2+ ion is also octahedrally coordinated by oxygen-containing ligands and Glu761 plays a similar role to that of Glu215. The carboxyphosphate and carbamoyl phosphate synthetic components, while topologically equivalent, are structurally different, as would be expected in light of their separate biochemical functions. |
==About this Structure== | ==About this Structure== | ||
| - | 1JDB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN, K, PO4, CL, GLN, ADP, ORN and NET as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbamoyl-phosphate_synthase_(glutamine-hydrolyzing) Carbamoyl-phosphate synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.5 6.3.5.5] Full crystallographic information is available from [http:// | + | 1JDB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=PO4:'>PO4</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=GLN:'>GLN</scene>, <scene name='pdbligand=ADP:'>ADP</scene>, <scene name='pdbligand=ORN:'>ORN</scene> and <scene name='pdbligand=NET:'>NET</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbamoyl-phosphate_synthase_(glutamine-hydrolyzing) Carbamoyl-phosphate synthase (glutamine-hydrolyzing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.5.5 6.3.5.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Holden, H | + | [[Category: Holden, H M.]] |
| - | [[Category: Raushel, F | + | [[Category: Raushel, F M.]] |
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
| - | [[Category: Thoden, J | + | [[Category: Thoden, J B.]] |
[[Category: Wesenberg, G.]] | [[Category: Wesenberg, G.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
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[[Category: synthase]] | [[Category: synthase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:19 2008'' |
Revision as of 11:21, 21 February 2008
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CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI
Overview
Carbamoyl phosphate synthetase catalyzes the formation of carbamoyl phosphate from one molecule of bicarbonate, two molecules of Mg2+ATP and one molecule of glutamine or ammonia depending upon the particular form of the enzyme under investigation. As isolated from Escherichia coli, the enzyme is an alpha,beta-heterodimer consisting of a small subunit that hydrolyzes glutamine and a large subunit that catalyzes the two required phosphorylation events. Here the three-dimensional structure of carbamoyl phosphate synthetase from E. coli refined to 2.1 A resolution with an R factor of 17.9% is described. The small subunit is distinctly bilobal with a catalytic triad (Cys269, His353 and Glu355) situated between the two structural domains. As observed in those enzymes belonging to the alpha/beta-hydrolase family, the active-site nucleophile, Cys269, is perched at the top of a tight turn. The large subunit consists of four structural units: the carboxyphosphate synthetic component, the oligomerization domain, the carbamoyl phosphate synthetic component and the allosteric domain. Both the carboxyphosphate and carbamoyl phosphate synthetic components bind Mn2+ADP. In the carboxyphosphate synthetic component, the two observed Mn2+ ions are both octahedrally coordinated by oxygen-containing ligands and are bridged by the carboxylate side chain of Glu299. Glu215 plays a key allosteric role by coordinating to the physiologically important potassium ion and hydrogen bonding to the ribose hydroxyl groups of ADP. In the carbamoyl phosphate synthetic component, the single observed Mn2+ ion is also octahedrally coordinated by oxygen-containing ligands and Glu761 plays a similar role to that of Glu215. The carboxyphosphate and carbamoyl phosphate synthetic components, while topologically equivalent, are structurally different, as would be expected in light of their separate biochemical functions.
About this Structure
1JDB is a Protein complex structure of sequences from Escherichia coli with , , , , , , and as ligands. Active as Carbamoyl-phosphate synthase (glutamine-hydrolyzing), with EC number 6.3.5.5 Full crystallographic information is available from OCA.
Reference
The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution., Thoden JB, Raushel FM, Benning MM, Rayment I, Holden HM, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):8-24. Epub 1999 Jan, 1. PMID:10089390
Page seeded by OCA on Thu Feb 21 13:21:19 2008
Categories: Carbamoyl-phosphate synthase (glutamine-hydrolyzing) | Escherichia coli | Protein complex | Holden, H M. | Raushel, F M. | Rayment, I. | Thoden, J B. | Wesenberg, G. | ADP | CL | GLN | K | MN | NET | ORN | PO4 | Amidotransferase | Ligase | Synthase
