Nucleotide sequence and analysis of the purA gene encoding adenylosuccinate synthetase of Escherichia coli K12.

Wolfe, Steven A.; Smith, John L.

doi:10.1016/s0021-9258(18)37402-7

Cited by 58 publications

(1 citation statement)

References 44 publications

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“…The method of Luzzati (1952) indicates an uncertainty in coordinates of 0.30 Å. The amino acid sequence used in refinement is identical to that reported by Silva et al (1995) and differs at position 416 (glycine instead of aspartate) from the amino acid sequence deduced from the nucleotide sequence (Wolfe & Smith, 1988). Results of the refinement are in Table 1.…”

Section: Resultsmentioning

confidence: 74%

Refined Crystal Structure of Adenylosuccinate Synthetase from Escherichia coli Complexed with Hydantocidin 5‘-Phosphate, GDP, HPO₄^2-, Mg²⁺, and Hadacidin^,

et al. 1996

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A crystal structure of adenylosuccinate synthetase from Escherichia coli, complexed with 5'-phosphate, GDP, HPO4(2-), Mg2+, and hadacidin at 100 K, has been refined to an Rfactor of 0.195 against data to 2.6 A resolution. Bond lengths and angles deviate from expected values by 0.012 A and 1.86 degrees, respectively. Lys 16 and backbone amides 15-17 and 42 interact with the phosphates of GDP, while Ser 414, Asp 333, and backbone amides 331 and 416 interact with the base. Mg2+ is octahedrally coordinated. Oxygen atoms from GDP, phosphate, and hadacidin define the equatorial plane of coordination of the Mg2+, while backbone carbonyl 40 and the side chain of Asp 13 are the apical ligands. HPO4(2-) hydrogen bonds with Lys 16, His 41, backbone amides 13, 40, and 224, and the base moiety of the hydantocidin inhibitor. The carboxylate of hadacidin interacts with Arg 303 and Thr 301; its N-formyl group coordinates to Mg2+, and its hydroxyl group hydrogen bonds with Asp 13. The 5'-phosphate of the hydantocidin inhibitor interacts with Asn 38, Thr 129, and Thr 239 but is approximately 3.5 A from Arg 143 (related by molecular 2-fold symmetry). The base moiety of hydantocidin 5'-phosphate hydrogen bonds to Gln 224 and participates in a hydrogen-bonded network that includes the phosphate molecule, several water molecules, and Asp 13. Hydantocidin 5'-phosphate, GDP, HPO4(2-), and Mg2+ may represent a set of synergistic inhibitors even more effective than the combination of IMP, GDP, NO3-, and Mg2+.

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Section: Resultsmentioning

confidence: 74%

Refined Crystal Structure of Adenylosuccinate Synthetase from Escherichia coli Complexed with Hydantocidin 5‘-Phosphate, GDP, HPO₄^2-, Mg²⁺, and Hadacidin^,

et al. 1996

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Adenylosuccinate Syntheatase: Recent Developments

Honzatko

Stayton

Formm

1999

Advances in Enzymology - And Related Areas of Molecular Biology

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8-(4-Bromo-2,3-dioxobutylthio)guanosine 5′-Triphosphate: A New Affinity Label for Purine Nucleotide Sites in Proteins

Lee

Gorrell

Fromm

et al. 1999

Archives of Biochemistry and Biophysics

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Nucleotide sequence and analysis of the purA gene encoding adenylosuccinate synthetase of Escherichia coli K12.

Cited by 58 publications

References 44 publications

Refined Crystal Structure of Adenylosuccinate Synthetase from Escherichia coli Complexed with Hydantocidin 5‘-Phosphate, GDP, HPO₄^2-, Mg²⁺, and Hadacidin^,

Refined Crystal Structure of Adenylosuccinate Synthetase from Escherichia coli Complexed with Hydantocidin 5‘-Phosphate, GDP, HPO₄^2-, Mg²⁺, and Hadacidin^,

Adenylosuccinate Syntheatase: Recent Developments

8-(4-Bromo-2,3-dioxobutylthio)guanosine 5′-Triphosphate: A New Affinity Label for Purine Nucleotide Sites in Proteins

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Nucleotide sequence and analysis of the purA gene encoding adenylosuccinate synthetase of Escherichia coli K12.

Cited by 58 publications

References 44 publications

Refined Crystal Structure of Adenylosuccinate Synthetase from Escherichia coli Complexed with Hydantocidin 5‘-Phosphate, GDP, HPO42-, Mg2+, and Hadacidin,

Refined Crystal Structure of Adenylosuccinate Synthetase from Escherichia coli Complexed with Hydantocidin 5‘-Phosphate, GDP, HPO42-, Mg2+, and Hadacidin,

Adenylosuccinate Syntheatase: Recent Developments

8-(4-Bromo-2,3-dioxobutylthio)guanosine 5′-Triphosphate: A New Affinity Label for Purine Nucleotide Sites in Proteins

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Product

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Refined Crystal Structure of Adenylosuccinate Synthetase from Escherichia coli Complexed with Hydantocidin 5‘-Phosphate, GDP, HPO₄^2-, Mg²⁺, and Hadacidin^,

Refined Crystal Structure of Adenylosuccinate Synthetase from Escherichia coli Complexed with Hydantocidin 5‘-Phosphate, GDP, HPO₄^2-, Mg²⁺, and Hadacidin^,