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| - | [[Image:1k92.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1k92| PDB=1k92 | SCENE= }} | | {{STRUCTURE_1k92| PDB=1k92 | SCENE= }} |
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| - | '''Crystal Structure of Uncomplexed E. coli Argininosuccinate Synthetase'''
| + | ===Crystal Structure of Uncomplexed E. coli Argininosuccinate Synthetase=== |
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| - | ==Overview==
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| - | BACKGROUND: 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. RESULTS: The crystal structure of E. coli AS (EAS) has been determined by the use of selenomethionine incorporation and MAD phasing. The structure has been refined at 1.6 A resolution in the absence of its substrates and at 2.0 A in the presence of aspartate and citrulline (EAS*CIT+ASP). Each monomer of this tetrameric protein has two structural domains: a nucleotide binding domain similar to that of the "N-type" ATP pyrophosphatase class of enzymes, and a novel catalytic/multimerization domain. The EAS*CIT+ASP structure clearly describes the binding of citrulline at the cleft between the two domains and of aspartate to a loop of the nucleotide binding domain, whereas homology modeling with the N-type ATP pyrophosphatases has provided the location of ATP binding. CONCLUSIONS: The first three-dimensional structures of AS are reported. The fold of the nucleotide binding domain confirms AS as the fourth structurally defined member of the N-type ATP pyrophosphatases. The structures identify catalytically important residues and suggest the requirement for a conformational change during the catalytic cycle. Sequence similarity between the bacterial and human enzymes has been used for providing insight into the structural and functional effects of observed clinical mutations.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11738042}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11738042 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11738042}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lemke, C T.]] | | [[Category: Lemke, C T.]] |
| | [[Category: N-type atp pyrophosphatase]] | | [[Category: N-type atp pyrophosphatase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:27:22 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 09:58:23 2008'' |
Revision as of 06:58, 2 July 2008
Template:STRUCTURE 1k92
Crystal Structure of Uncomplexed E. coli Argininosuccinate Synthetase
Template:ABSTRACT PUBMED 11738042
About this Structure
1K92 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The 1.6 A crystal structure of E. coli argininosuccinate synthetase suggests a conformational change during catalysis., Lemke CT, Howell PL, Structure. 2001 Dec;9(12):1153-64. PMID:11738042
Page seeded by OCA on Wed Jul 2 09:58:23 2008
