1kp3: Difference between revisions
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[[Image:1kp3.jpg|left|200px]] | [[Image:1kp3.jpg|left|200px]] | ||
'''Crystal Structure of E. coli Argininosuccinate Synthetase in Complex with ATP and Citrulline''' | {{Structure | ||
|PDB= 1kp3 |SIZE=350|CAPTION= <scene name='initialview01'>1kp3</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=CIR:CITRULLINE'>CIR</scene> and <scene name='pdbligand=GAI:GUANIDINE'>GAI</scene> | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Argininosuccinate_synthase Argininosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.5 6.3.4.5] | |||
|GENE= ARGG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |||
}} | |||
'''Crystal Structure of E. coli Argininosuccinate Synthetase in Complex with ATP and Citrulline''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1KP3 is a [ | 1KP3 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=1KP3 OCA]. | ||
==Reference== | ==Reference== | ||
Substrate induced conformational changes in argininosuccinate synthetase., Lemke CT, Howell PL, J Biol Chem. 2002 Apr 12;277(15):13074-81. Epub 2002 Jan 23. PMID:[http:// | Substrate induced conformational changes in argininosuccinate synthetase., Lemke CT, Howell PL, J Biol Chem. 2002 Apr 12;277(15):13074-81. Epub 2002 Jan 23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11809762 11809762] | ||
[[Category: Argininosuccinate synthase]] | [[Category: Argininosuccinate synthase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: n-type atp pyrophosphatase]] | [[Category: n-type atp pyrophosphatase]] | ||
''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 12:20:17 2008'' | ||
Revision as of 13:20, 20 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , and | ||||||
| Gene: | ARGG (Escherichia coli) | ||||||
| Activity: | Argininosuccinate synthase, with EC number 6.3.4.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of E. coli Argininosuccinate Synthetase in Complex with ATP and Citrulline
OverviewOverview
Argininosuccinate synthetase (AS) is the rate-limiting enzyme of both the urea and arginine-citrulline cycles. In mammals, deficiency of AS leads to citrullinemia, a debilitating and often fatal autosomal recessive urea cycle disorder, whereas its overexpression for sustained nitric oxide production via the arginine-citrulline cycle leads to the potentially fatal hypotension associated with septic and cytokine-induced circulatory shock. The crystal structures of Escherichia coli argininosuccinate synthetase (EAS) in complex with ATP and with ATP and citrulline have been determined at 2.0-A resolution. These are the first EAS structures to be solved in the presence of a nucleotide substrate and clearly identify the residues that interact with both ATP and citrulline. Two distinct conformations are revealed for ATP, both of which are believed to be catalytically relevant. In addition, comparisons of these EAS structures with those of the apoenzyme and EAS complexed with aspartate and citrulline (Lemke, C. T., and Howell, P. L. (2001) Structure (Lond.) 9, 1153-1164) provide structural evidence of ATP-induced conformational changes in the nucleotide binding domain. Combined, these structures also provide structural explanations of some of the observed kinetic properties of the enzyme and have enabled a detailed enzymatic mechanism of AS catalysis to be proposed.
About this StructureAbout this Structure
1KP3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Substrate induced conformational changes in argininosuccinate synthetase., Lemke CT, Howell PL, J Biol Chem. 2002 Apr 12;277(15):13074-81. Epub 2002 Jan 23. PMID:11809762
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