The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site (Q27736436)

2

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Y Karimi-Nejad

3

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J van der Zwan

4

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M Mariani

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D Schipper

6

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R Boelens

Serine Proteases: Structure and Mechanism of Catalysis

7

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language of work or name

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15 April 1997

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published in

Structure

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volume

5

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page(s)

521-32

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issue

4

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cites work

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Structural basis of substrate specificity in the serine proteases

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Protein engineering of subtilisin BPN': enhanced stabilization through the introduction of two cysteines to form a disulfide bond

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Incorporation of a stabilizing Ca(2+)-binding loop into subtilisin BPN'

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Engineering a novel specificity in subtilisin BPN'

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Directed evolution of a subtilisin with calcium-independent stability.

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Proteases of enhanced stability: characterization of a thermostable variant of subtilisin

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Rational protein engineering and industrial application: structure prediction by homology and rational design of protein-variants with improved ‘washing performance’ — the alkaline protease from Bacillus alcalophilus

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Generation of soluble interleukin-1 receptor from an immunoadhesin by specific cleavage

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Designing subtilisin BPN' to cleave substrates containing dibasic residues

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7 January 2021

Crystal structure of the high-alkaline serine protease PB92 from Bacillus alcalophilus

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7 January 2021

Structure of Subtilisin BPN′ at 2.5 Å Resolution

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7 January 2021

Crystal and molecular structure of chymotrypsin inhibitor 2 from barley seeds in complex with subtilisin Novo

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7 January 2021

Refined crystal structures of subtilisin novo in complex with wild-type and two mutant eglins. Comparison with other serine proteinase inhibitor complexes

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7 January 2021

Crystal and molecular structure of the inhibitor eglin from leeches in complex with subtilisin Carlsberg

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The high-resolution X-ray crystal structure of the complex formed between subtilisin Carlsberg and eglin c, an elastase inhibitor from the leech Hirudo medicinalis. Structural analysis, subtilisin structure and interface geometry

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The refined crystal structure of subtilisin Carlsberg at 2.5 A resolution

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Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 A resolution and comparison of two crystal forms that differ in calcium content

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7 January 2021

Synchrotron X-ray data collection and restrained least-squares refinement of the crystal structure of proteinase K at 1.5 A resolution

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X-ray and model-building studies on the specificity of the active site of proteinase K

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7 January 2021

Crystal structure of the alkaline proteinase Savinase™ from Bacillus lentus at 1.4 Å resolution

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The crystal structure of the Bacillus lentus alkaline protease, subtilisin BL, at 1.4 A resolution

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Significance of hydrophobic S4-P4 interactions in subtilisin 309 from Bacillus lentus

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Mutational replacements of the amino acid residues forming the hydrophobic S4 binding pocket of subtilisin 309 from Bacillus lentus

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Engineering surface charges in a subtilisin: the effects on electrophoretic and ion-exchange behaviour

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X-ray structure determination and comparison of two crystal forms of a variant (Asn115Arg) of the alkaline protease from Bacillus alcalophilus refined at 1.85 Å resolution

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Structural comparison of two serine proteinase-protein inhibitor complexes: eglin-c-subtilisin Carlsberg and CI-2-subtilisin Novo

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(1)H, (13)C and (15)N NMR backbone assignments of the 269-residue serine protease PB92 from Bacillus alcalophilus.

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Complete 1H, 13C and 15N NMR assignments and secondary structure of the 269-residue serine protease PB92 from Bacillus alcalophilus

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Role of a Buried Acid Group in the Mechanism of Action of Chymotrypsin

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Rational modification of enzyme catalysis by engineering surface charge

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Electrostatic effects on modification of charged groups in the active site cleft of subtilisin by protein engineering

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Recruitment of substrate-specificity properties from one enzyme into a related one by protein engineering

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The engineering of binding affinity at metal ion binding sites for the stabilization of proteins: subtilisin as a test case

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7 January 2021

Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfolding

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7 January 2021

High-resolution structure of calcium-loaded calbindin D9k

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Solution structure of (Cd2+)1-calbindin D9k reveals details of the stepwise structural changes along the Apo-->(Ca2+)II1-->(Ca2+)I,II2 binding pathway

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7 January 2021

Neutron structure of subtilisin BPN': effects of chemical environment on hydrogen-bonding geometries and the pattern of hydrogen-deuterium exchange in secondary structure elements.

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Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling

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P NMR and mass spectrometry of atropinesterase and some serine proteases phosphorylated with a transition-state analogue

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Detection of nuclear Overhauser effects between degenerate amide proton resonances by heteronuclear three-dimensional NMR spectroscopy

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Measurement of the exchange rates of rapidly exchanging amide protons: Application to the study of calmodulin and its complex with a myosin light chain kinase fragment

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Improved HSQC experiments for the observation of exchange broadened signals.

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Determination of three-dimensional structures of proteins from interproton distance data by hybrid distance geometry-dynamical simulated annealing calculations

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7 January 2021

A calculation strategy for the structure determination of symmetric dimers by 1H NMR.

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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

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Identifiers

DOI

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Fatcat ID

release_rc4lng7uk5a6hi5oor4jaudkbe

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Fatcat

https://api.fatcat.wiki/v0/release/rc4lng7uk5a6hi5oor4jaudkbe

24 November 2022