The crystal structure of diglycine sulphate monohydrate

Cano, F. H.; Martínez-Carrera, S.

doi:10.1107/s0567740874007904

Cited by 9 publications

(2 citation statements)

References 2 publications

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“…Lying close to Asp151, but outside the substrate-binding site, is a second sulfate anion that forms a hydrogen bond with the N 1 atom of His150 (SBS2). The distance of closest approach between the carboxylate O atom of the side chain of Asp151 and an O atom of this sulfate falls in the range 2.71-3.41 Å in the four monomers; these distances are consistent with a neutral carboxyl group (Vilminot et al, 1974;Cano & Martínez-Carrera, 1974;Vilminot & Philippot, 1976;Capasso et al, 1983;Nagashima et al, 1992;Srinivasan et al, 2001a,b). Sequence analysis of clinical isolates of influenza virus have identified Asp151 as the most variable of the conserved residues (McKimm-Breschkin et al, 2003); substitution by residues incapable of acting as an acid (asparagine, valine and glycine), however, deny Asp151 a critical role in catalysis.…”

Section: Sulfate-binding Sitessupporting

confidence: 59%

Structure of a calcium-deficient form of influenza virus neuraminidase: implications for substrate binding

Smith

Huyton

Joosten

et al. 2006

Acta Crystallogr D Biol Crystallogr

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The X-ray structure of influenza virus neuraminidase (NA) isolated from whale, subtype N9, has been determined at 2.2 A resolution and contains a tetrameric protein in the asymmetric unit. In structures of NA determined previously, a calcium ion is observed to coordinate amino acids near the substrate-binding site. In three of the NA monomers determined here this calcium is absent, resulting in structural alterations near the substrate-binding site. These changes affect the conformation of residues that participate in several key interactions between the enzyme and substrate and provide at a molecular level the basis of the structural and functional role of calcium in substrate and inhibitor binding. Several sulfate ions were identified in complex with the protein. These are located in the active site, occupying the space reserved for the substrate (sialic acid) carboxylate, and in positions leading away from the substrate-binding site. These sites offer a new opportunity for the design of inhibitors of influenza virus NA.

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Section: Sulfate-binding Sitessupporting

confidence: 59%

Structure of a calcium-deficient form of influenza virus neuraminidase: implications for substrate binding

Smith

Huyton

Joosten

et al. 2006

Acta Crystallogr D Biol Crystallogr

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“…The size of the crystal was 20x10x10 mm 3 and growth period was taken around 25 days. The chosen crystal was already grown in the earlier century [11][12][13]. The DGSM single crystal was shown in Fig.1.…”

Section: Methodsmentioning

confidence: 99%

Synthesis, Growth, Structural, Optical and Electrical Properties of Di-Glycine Sulfate Monohydrate Single Crystals

Ramamoorthy¹,

Ángel²,

Manimaran³

et al. 2019

IJASE

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Growth investigations of single crystal sulphates containing molecular glycine groups

Szczepańaska

1976

Cryst Res and Technol

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Investigations on the optimalisation of the growth conditions of single crystals containing molecular glycine groups were performed and depending on the pH-value of the solution, crystals of triglycine sulphate, diglycine sulphate or diglycine sulphate monohydrate can be grown. The optimal pH-value for triglycine sulphate growing was found to be 1.5. Es wurden Untersuchungen uber die Optimierung der Wachstumsbedingungen fiirEinkristalle, die molekulare Glyzingruppen enthalten, und iiber die Wachstumsabhangigkeit der Triglyzinsulfat-, Diglyzinsulfat-und Diglyzinsulfatmonohydrat-Einkristalle vom pH-Wert der Lijsung durchgefiihrt. I m Falle des Triglyzinsulfats betriigt der optimale pH-Wert 1,5.

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The crystal structure of diglycine sulphate monohydrate

Cited by 9 publications

References 2 publications

Structure of a calcium-deficient form of influenza virus neuraminidase: implications for substrate binding

Structure of a calcium-deficient form of influenza virus neuraminidase: implications for substrate binding

Synthesis, Growth, Structural, Optical and Electrical Properties of Di-Glycine Sulfate Monohydrate Single Crystals

Growth investigations of single crystal sulphates containing molecular glycine groups

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