(Q27632940)

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1.3 A structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family

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1.3 A structure of arylsulfatase from Pseudomonas aeruginosa establishes the catalytic mechanism of sulfate ester cleavage in the sulfatase family (English)

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Pseudomonas aeruginosa

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author name string

I Boltes

1

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H Czapinska

2

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A Kahnert

3

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R von Bülow

4

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T Dierks

5

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B Schmidt

6

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K von Figura

7

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M A Kertesz

8

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I Usón

9

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publication date

June 2001

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9

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6

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483-91

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The sulfatase gene family

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A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency

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The evolutionary conservation of a novel protein modification, the conversion of cysteine to serinesemialdehyde in arylsulfatase from Volvox carteri

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Conversion of cysteine to formylglycine: A protein modification in the endoplasmic reticulum

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Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated from a serine

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Purification and characterization of the arylsulfatase synthesized by Pseudomonas aeruginosa PAO during growth in sulfate-free medium and cloning of the arylsulfatase gene (atsA)

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Posttranslational formation of formylglycine in prokaryotic sulfatases by modification of either cysteine or serine

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Regulation of the sulfate starvation response in Pseudomonas aeruginosa: role of cysteine biosynthetic intermediates

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Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis

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Structure of a human lysosomal sulfatase

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Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis

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Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis

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Amino acid residues forming the active site of arylsulfatase A. Role in catalytic activity and substrate binding

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Processing of X-ray diffraction data collected in oscillation mode

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[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods.

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Automated protein model building combined with iterative structure refinement

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Assessment of phase accuracy by cross validation: the free R value. Methods and applications

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1.7 A structure of the stabilized REIv mutant T39K. Application of local NCS restraints

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An extensively modified version of MolScript that includes greatly enhanced coloring capabilities

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