(Q27641613)

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Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions

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Crystal structure of M tuberculosis ABC phosphate transport receptor: specificity and charge compensation dominated by ion-dipole interactions (English)

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crystal structure

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Mycobacterium tuberculosis

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author name string

Nand K Vyas

1

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Meenakshi N Vyas

2

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Florante A Quiocho

3

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publication date

July 2003

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11

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7

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765-74

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Structure and mapping of antigenic domains of protein antigen b, a 38,000-molecular-weight protein of Mycobacterium tuberculosis

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Dipoles localized at helix termini of proteins stabilize charges

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Crystallization and preliminary X-ray crystallographic analysis of the 38-kDa immunodominant antigen of Mycobacterium tuberculosis

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The Structure of the Potassium Channel: Molecular Basis of K+ Conduction and Selectivity

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X-ray structure of a ClC chloride channel at 3.0 A reveals the molecular basis of anion selectivity

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The 38-kDa protein of Mycobacterium tuberculosis: a review

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Dominant role of local dipoles in stabilizing uncompensated charges on a sulfate sequestered in a periplasmic active transport protein

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The alpha-helix dipole and the properties of proteins

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Crystal structure of the molybdate binding protein ModA

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The association between a negatively charged ligand and the electronegative binding pocket of its receptor

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Sulfate-binding protein dislikes protonated oxyacids. A molecular explanation.

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Negatively charged anabaena flavodoxin residues (Asp144 and Glu145) are important for reconstitution of cytochrome P450 17alpha-hydroxylase activity.

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T cell responses to a mixture of Mycobacterium tuberculosis peptides with complementary HLA-DR binding profiles

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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Ligand size is a major determinant of specificity in periplasmic oxyanion-binding proteins: the 1.2 A resolution crystal structure of Azotobacter vinelandii ModA

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Negative electrostatic surface potential of protein sites specific for anionic ligands

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Dominant role of local dipolar interactions in phosphate binding to a receptor cleft with an electronegative charge surface: equilibrium, kinetic, and crystallographic studies

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Three different putative phosphate transport receptors are encoded by the Mycobacterium tuberculosis genome and are present at the surface of Mycobacterium bovis BCG

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High specificity of a phosphate transport protein determined by hydrogen bonds

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A novel all helix fold of the AP180 amino-terminal domain for phosphoinositide binding and clathrin assembly in synaptic vesicle endocytosis

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Sulphate sequestered in the sulphate-binding protein of Salmonella typhimurium is bound solely by hydrogen bonds

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Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes

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Stabilization of charges on isolated ionic groups sequestered in proteins by polarized peptide units

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Crystal structure of constitutive endothelial nitric oxide synthase: a paradigm for pterin function involving a novel metal center

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Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution

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The nature of the immunogen determines the specificity of antibodies and T cells to selected peptides of the 38 kDa mycobacterial antigen

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A low energy short hydrogen bond in very high resolution structures of protein receptor--phosphate complexes

1 reference

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Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor

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Lipoprotein antigens of Mycobacterium tuberculosis

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Identifiers

10.1016/S0969-2126(03)00109-6

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Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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