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| | {{STRUCTURE_1gso| PDB=1gso | SCENE= }} | | {{STRUCTURE_1gso| PDB=1gso | SCENE= }} |
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| - | '''GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE (GAR-SYN) FROM E. COLI.'''
| + | ===GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE (GAR-SYN) FROM E. COLI.=== |
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| - | ==Overview==
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| - | Glycinamide ribonucleotide synthetase (GAR-syn) catalyzes the second step of the de novo purine biosynthetic pathway; the conversion of phosphoribosylamine, glycine, and ATP to glycinamide ribonucleotide (GAR), ADP, and Pi. GAR-syn containing an N-terminal polyhistidine tag was expressed as the SeMet incorporated protein for crystallographic studies. In addition, the protein as isolated contains a Pro294Leu mutation. This protein was crystallized, and the structure solved using multiple-wavelength anomalous diffraction (MAD) phase determination and refined to 1.6 A resolution. GAR-syn adopts an alpha/beta structure that consists of four domains labeled N, A, B, and C. The N, A, and C domains are clustered to form a large central core structure whereas the smaller B domain is extended outward. Two hinge regions, which might readily facilitate interdomain movement, connect the B domain and the main core. A search of structural databases showed that the structure of GAR-syn is similar to D-alanine:D-alanine ligase, biotin carboxylase, and glutathione synthetase, despite low sequence similarity. These four enzymes all utilize similar ATP-dependent catalytic mechanisms even though they catalyze different chemical reactions. Another ATP-binding enzyme with low sequence similarity but unknown function, synapsin Ia, was also found to share high structural similarity with GAR-syn. Interestingly, the GAR-syn N domain shows similarity to the N-terminal region of glycinamide ribonucleotide transformylase and several dinucleotide-dependent dehydrogenases. Models of ADP and GAR binding were generated based on structure and sequence homology. On the basis of these models, the active site lies in a cleft between the large domain and the extended B domain. Most of the residues that facilitate ATP binding belong to the A or B domains. The N and C domains appear to be largely responsible for substrate specificity. The structure of GAR-syn allows modeling studies of possible channeling complexes with PPRP amidotransferase.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9843369}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9843369 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9843369}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Purine de novo biosynthetic pathway]] | | [[Category: Purine de novo biosynthetic pathway]] |
| | [[Category: Substrate channeling]] | | [[Category: Substrate channeling]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:57:40 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:00:41 2008'' |
Revision as of 03:00, 1 July 2008
Template:STRUCTURE 1gso
GLYCINAMIDE RIBONUCLEOTIDE SYNTHETASE (GAR-SYN) FROM E. COLI.
Template:ABSTRACT PUBMED 9843369
About this Structure
1GSO is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli., Wang W, Kappock TJ, Stubbe J, Ealick SE, Biochemistry. 1998 Nov 10;37(45):15647-62. PMID:9843369
Page seeded by OCA on Tue Jul 1 06:00:41 2008
