Structure and function of Caulobacter crescentus aldose–aldose oxidoreductase

2015 ◽  
Vol 472 (3) ◽  
pp. 297-307 ◽  
Author(s):  
Helena Taberman ◽  
Martina Andberg ◽  
Anu Koivula ◽  
Nina Hakulinen ◽  
Merja Penttilä ◽  
...  
Keyword(s):  
Reaction Mechanism ◽  
Crystal Structures ◽  
Molecular Basis ◽  
Caulobacter Crescentus ◽  
Substrate Binding ◽  
Structure And Function ◽  
Sugar Alcohols ◽  
And Function

We solved the crystal structures of Caulobacter crescentus aldose–aldose oxidoreductase complexed with its NADP(H) cofactor, different saccharides and sugar alcohols. The structures demonstrate the molecular basis for substrate binding and allowed us to present a reaction mechanism for the enzyme.

Crystal Structures of Fragments D and Double-D from Fibrinogen and Fibrin

1999 ◽  
Vol 82 (08) ◽  
pp. 271-276 ◽  
Author(s):  
Glen Spraggon ◽  
Stephen Everse ◽  
Russell Doolittle
Keyword(s):  
Electron Microscopy ◽  
High Resolution ◽  
Crystal Structures ◽  
Structure And Function ◽  
X Ray ◽  
Long Period ◽  
And Function

IntroductionAfter a long period of anticipation,1 the last two years have witnessed the first high-resolution x-ray structures of fragments from fibrinogen and fibrin.2-7 The results confirmed many aspects of fibrinogen structure and function that had previously been inferred from electron microscopy and biochemistry and revealed some unexpected features. Several matters have remained stubbornly unsettled, however, and much more work remains to be done. Here, we review several of the most significant findings that have accompanied the new x-ray structures and discuss some of the problems of the fibrinogen-fibrin conversion that remain unresolved. * Abbreviations: GPR—Gly-Pro-Arg-derivatives; GPRPam—Gly-Pro-Arg-Pro-amide; GHRPam—Gly-His-Arg-Pro-amide

scholarly journals GENETIC MAPPING OF GENES REQUIRED FOR MOTILITY IN CAULOBACTER CRESCENTUS

Genetics ◽  
1984 ◽  
Vol 108 (3) ◽  
pp. 523-532
Author(s):  
Bert Ely ◽  
Ronda H Croft ◽  
Connie J Gerardot
Keyword(s):  
Genetic Mapping ◽  
Caulobacter Crescentus ◽  
Pleiotropic Effect ◽  
Structure And Function ◽  
Bacteriophage Resistance ◽  
And Function ◽  
Chromosomal Map ◽  
Bacterial Systems

ABSTRACT Mutations in more than 30 genes affect motility in Caulobacter crescentus. We have determined the chromosomal map locations for 27 genes involved in flagellar morphogenesis (fla), three genes involved in flagellar function (mot), and three genes that have a pleiotropic effect on both motility and bacteriophage resistance (ple). Three multigene clusters have been detected at widely separated chromosomal locations, but in addition, there are 12 fla and mot genes that are found at eight additional sites scattered around the C. cresentus chromosome. Thus, there is more scatter of genes involved in flagellar structure and function than has been observed in other bacterial systems.

Chitosanase from Streptomyces sp. strain N174: a comparative review of its structure and function

1997 ◽  
Vol 75 (6) ◽  
pp. 687-696 ◽  
Author(s):  
Tamo Fukamizo ◽  
Ryszard Brzezinski
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Substrate Binding ◽  
Structure And Function ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Amino Acid Residues ◽  
Streptomyces Sp ◽  
Binding Cleft ◽  
And Function

Novel information on the structure and function of chitosanase, which hydrolyzes the beta -1,4-glycosidic linkage of chitosan, has accumulated in recent years. The cloning of the chitosanase gene from Streptomyces sp. strain N174 and the establishment of an efficient expression system using Streptomyces lividans TK24 have contributed to these advances. Amino acid sequence comparisons of the chitosanases that have been sequenced to date revealed a significant homology in the N-terminal module. From energy minimization based on the X-ray crystal structure of Streptomyces sp. strain N174 chitosanase, the substrate binding cleft of this enzyme was estimated to be composed of six monosaccharide binding subsites. The hydrolytic reaction takes place at the center of the binding cleft with an inverting mechanism. Site-directed mutagenesis of the carboxylic amino acid residues that are conserved revealed that Glu-22 and Asp-40 are the catalytic residues. The tryptophan residues in the chitosanase do not participate directly in the substrate binding but stabilize the protein structure by interacting with hydrophobic and carboxylic side chains of the other amino acid residues. Structural and functional similarities were found between chitosanase, barley chitinase, bacteriophage T4 lysozyme, and goose egg white lysozyme, even though these proteins share no sequence similarities. This information can be helpful for the design of new chitinolytic enzymes that can be applied to carbohydrate engineering, biological control of phytopathogens, and other fields including chitinous polysaccharide degradation. Key words: chitosanase, amino acid sequence, overexpression system, reaction mechanism, site-directed mutagenesis.

scholarly journals Structure and function of cytochromes P450:a comparative analysis of three crystal structures

Structure ◽  
1995 ◽  
Vol 3 (1) ◽  
pp. 41-62 ◽  
Author(s):  
Charles A Hasemann ◽  
Ravi G Kurumbail ◽  
Sekhar S Boddupalli ◽  
Julian A Peterson ◽  
Johann Deisenhofer
Keyword(s):  
Comparative Analysis ◽  
Crystal Structures ◽  
Cytochromes P450 ◽  
Structure And Function ◽  
And Function

scholarly journals Exotoxins of Staphylococcus aureus

2000 ◽  
Vol 13 (1) ◽  
pp. 16-34 ◽  
Author(s):  
Martin M. Dinges ◽  
Paul M. Orwin ◽  
Patrick M. Schlievert
Keyword(s):  
Staphylococcus Aureus ◽  
Toxic Shock Syndrome ◽  
Molecular Basis ◽  
Molecular Mechanisms ◽  
Food Poisoning ◽  
Structure And Function ◽  
Toxic Shock ◽  
The Family ◽  
Toxic Shock Syndrome Toxin ◽  
And Function

SUMMARY This article reviews the literature regarding the structure and function of two types of exotoxins expressed by Staphylococcus aureus, pyrogenic toxin superantigens (PTSAgs) and hemolysins. The molecular basis of PTSAg toxicity is presented in the context of two diseases known to be caused by these exotoxins: toxic shock syndrome and staphylococcal food poisoning. The family of staphylococcal PTSAgs presently includes toxic shock syndrome toxin-1 (TSST-1) and most of the staphylococcal enterotoxins (SEs) (SEA, SEB, SEC, SED, SEE, SEG, and SEH). As the name implies, the PTSAgs are multifunctional proteins that invariably exhibit lethal activity, pyrogenicity, superantigenicity, and the capacity to induce lethal hypersensitivity to endotoxin. Other properties exhibited by one or more staphylococcal PTSAgs include emetic activity (SEs) and penetration across mucosal barriers (TSST-1). A detailed review of the molecular mechanisms underlying the toxicity of the staphylococcal hemolysins is also presented.

A stochastic roadmap method to model protein structural transitions

Robotica ◽  
2015 ◽  
Vol 34 (8) ◽  
pp. 1705-1733 ◽  
Author(s):  
Kevin Molloy ◽  
Rudy Clausen ◽  
Amarda Shehu
Keyword(s):  
Protein Structure ◽  
Molecular Basis ◽  
Structure And Function ◽  
Structural Transitions ◽  
Simulation Framework ◽  
Human Disorders ◽  
Model Protein ◽  
And Function ◽  
The Impact

SUMMARYEvidence is emerging that the role of protein structure in disease needs to be rethought. Sequence mutations in proteins are often found to affect the rate at which a protein switches between structures. Modeling structural transitions in wildtype and variant proteins is central to understanding the molecular basis of disease. This paper investigates an efficient algorithmic realization of the stochastic roadmap simulation framework to model structural transitions in wildtype and variants of proteins implicated in human disorders. Our results indicate that the algorithm is able to extract useful information on the impact of mutations on protein structure and function.

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