1jdb

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[[Image:1jdb.gif|left|200px]]
[[Image:1jdb.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1jdb |SIZE=350|CAPTION= <scene name='initialview01'>1jdb</scene>, resolution 2.1&Aring;
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The line below this paragraph, containing "STRUCTURE_1jdb", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ADP:ADENOSINE-5&#39;-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLN:GLUTAMINE'>GLN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=NET:TETRAETHYLAMMONIUM+ION'>NET</scene>, <scene name='pdbligand=ORN:ORNITHINE'>ORN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1jdb| PDB=1jdb | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jdb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdb OCA], [http://www.ebi.ac.uk/pdbsum/1jdb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jdb RCSB]</span>
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}}
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'''CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI'''
'''CARBAMOYL PHOSPHATE SYNTHETASE FROM ESCHERICHIA COLI'''
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/10089390 10089390]
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:[http://www.ncbi.nlm.nih.gov/pubmed/10089390 10089390]
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[[Category: Carbamoyl-phosphate synthase (glutamine-hydrolyzing)]]
 
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Thoden, J B.]]
[[Category: Thoden, J B.]]
[[Category: Wesenberg, G.]]
[[Category: Wesenberg, G.]]
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[[Category: amidotransferase]]
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[[Category: Amidotransferase]]
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[[Category: ligase]]
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[[Category: Ligase]]
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[[Category: synthase]]
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[[Category: Synthase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:05:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:31:59 2008''
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Revision as of 18:05, 2 May 2008

Image:1jdb.gif

Template:STRUCTURE 1jdb

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. 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 Fri May 2 21:05:09 2008

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