Literature DB >> 1899664

Three-dimensional structure of the elastase of Pseudomonas aeruginosa at 1.5-A resolution.

M M Thayer1, K M Flaherty, D B McKay.   

Abstract

Pseudomonas aeruginosa elastase (PAE) is a zinc metalloprotease with 301 amino acids. We have crystallized and solved the three-dimensional structure of PAE, using data to 1.5-A resolution, and have refined the native molecular structure to R = 0.188. The overall tertiary structure of the PAE molecule is similar to that of thermolysin, with which it shares 28% amino acid sequence identity. Nearly all of the active site residues that might potentially interact with substrates are identical in the two proteins. However, the active site cleft is significantly more "open" in PAE than in thermolysin.

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Year:  1991        PMID: 1899664     DOI: 10.2210/pdb1ezm/pdb

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  54 in total

1.  Role of intermolecular disulfide bonds of the organic solvent-stable PST-01 protease in its organic solvent stability.

Authors:  H Ogino; T Uchiho; J Yokoo; R Kobayashi; R Ichise; H Ishikawa
Journal:  Appl Environ Microbiol       Date:  2001-02       Impact factor: 4.792

2.  Proteome analysis of the effect of mucoid conversion on global protein expression in Pseudomonas aeruginosa strain PAO1 shows induction of the disulfide bond isomerase, dsbA.

Authors:  S Malhotra; L A Silo-Suh; K Mathee; D E Ohman
Journal:  J Bacteriol       Date:  2000-12       Impact factor: 3.490

3.  Highly sensitive quenched fluorescent substrate of Legionella major secretory protein (msp) based on its structural analysis.

Authors:  Hervé Poras; Sophie Duquesnoy; Emilie Dange; Anthony Pinon; Michèle Vialette; Marie-Claude Fournié-Zaluski; Tanja Ouimet
Journal:  J Biol Chem       Date:  2012-04-23       Impact factor: 5.157

4.  A substitution at His-120 in the LasA protease of Pseudomonas aeruginosa blocks enzymatic activity without affecting propeptide processing or extracellular secretion.

Authors:  J K Gustin; E Kessler; D E Ohman
Journal:  J Bacteriol       Date:  1996-11       Impact factor: 3.490

5.  Characterization of a periplasmic thiol:disulfide interchange protein required for the functional maturation of secreted virulence factors of Vibrio cholerae.

Authors:  J A Peek; R K Taylor
Journal:  Proc Natl Acad Sci U S A       Date:  1992-07-01       Impact factor: 11.205

Review 6.  What can be inferred from bacterium-nanoparticle interactions about the potential consequences of environmental exposure to nanoparticles?

Authors:  Andrew L Neal
Journal:  Ecotoxicology       Date:  2008-05-03       Impact factor: 2.823

Review 7.  Bacterial extracellular zinc-containing metalloproteases.

Authors:  C C Häse; R A Finkelstein
Journal:  Microbiol Rev       Date:  1993-12

Review 8.  Expression of virus-encoded proteinases: functional and structural similarities with cellular enzymes.

Authors:  W G Dougherty; B L Semler
Journal:  Microbiol Rev       Date:  1993-12

9.  Cold adaptation of zinc metalloproteases in the thermolysin family from deep sea and arctic sea ice bacteria revealed by catalytic and structural properties and molecular dynamics: new insights into relationship between conformational flexibility and hydrogen bonding.

Authors:  Bin-Bin Xie; Fei Bian; Xiu-Lan Chen; Hai-Lun He; Jun Guo; Xiang Gao; Yin-Xin Zeng; Bo Chen; Bai-Cheng Zhou; Yu-Zhong Zhang
Journal:  J Biol Chem       Date:  2009-01-30       Impact factor: 5.157

10.  Pseudomonas aeruginosa lasB1 mutants produce an elastase, substituted at active-site His-223, that is defective in activity, processing, and secretion.

Authors:  K S McIver; J C Olson; D E Ohman
Journal:  J Bacteriol       Date:  1993-07       Impact factor: 3.490

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