Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria

1997 ◽  
Vol 4 (12) ◽  
pp. 995-1000 ◽  
Author(s):  
Heidi Erlandsen ◽  
Fabrizia Fusetti ◽  
Aurora Martinez ◽  
Edward Hough ◽  
Torgeir Flatmark ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Domain ◽  
Phenylalanine Hydroxylase ◽  
Structural Basis ◽  
Human Phenylalanine Hydroxylase

scholarly journals X-Ray Crystal Structure of the Multidomain Endoglucanase Cel9G from Clostridium cellulolyticum Complexed with Natural and Synthetic Cello-Oligosaccharides

2003 ◽  
Vol 185 (14) ◽  
pp. 4127-4135 ◽  
Author(s):  
David Mandelman ◽  
Anne Belaich ◽  
J. P. Belaich ◽  
Nushin Aghajari ◽  
Hugues Driguez ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Domain ◽  
Cellulose Degradation ◽  
Cellulase Activity ◽  
Structural Basis ◽  
Crystalline Cellulose ◽  
X Ray ◽  
Clostridium Cellulolyticum ◽  
Active Site Cleft ◽  
Cellulose Binding

ABSTRACT Complete cellulose degradation is the first step in the use of biomass as a source of renewable energy. To this end, the engineering of novel cellulase activity, the activity responsible for the hydrolysis of the β-1,4-glycosidic bonds in cellulose, is a topic of great interest. The high-resolution X-ray crystal structure of a multidomain endoglucanase from Clostridium cellulolyticum has been determined at a 1.6-Å resolution. The endoglucanase, Cel9G, is comprised of a family 9 catalytic domain attached to a family IIIc cellulose-binding domain. The two domains together form a flat platform onto which crystalline cellulose is suggested to bind and be fed into the active-site cleft for endolytic hydrolysis. To further dissect the structural basis of cellulose binding and hydrolysis, the structures of Cel9G in the presence of cellobiose, cellotriose, and a DP-10 thio-oligosaccharide inhibitor were resolved at resolutions of 1.7, 1.8, and 1.9 Å, respectively.

scholarly journals Crystal structure of glycosyltrehalose synthase fromSulfolobus shibataeDSM5389

2018 ◽  
Vol 74 (11) ◽  
pp. 741-746
Author(s):  
Nobuo Okazaki ◽  
Michael Blaber ◽  
Ryota Kuroki ◽  
Taro Tamada
Keyword(s):  
Crystal Structure ◽  
Amino Acids ◽  
Catalytic Mechanism ◽  
Catalytic Domain ◽  
Structural Basis ◽  
Hyperthermophilic Archaeon ◽  
X Ray ◽  
X Ray Crystallography ◽  
Sulfolobus Shibatae ◽  
Glucosidic Bond

Glycosyltrehalose synthase (GTSase) converts the glucosidic bond between the last two glucose residues of amylose from an α-1,4 bond to an α-1,1 bond, generating a nonreducing glycosyl trehaloside, in the first step of the biosynthesis of trehalose. To better understand the structural basis of the catalytic mechanism, the crystal structure of GTSase from the hyperthermophilic archaeonSulfolobus shibataeDSM5389 (5389-GTSase) has been determined to 2.4 Å resolution by X-ray crystallography. The structure of 5389-GTSase can be divided into five domains. The central domain contains the (β/α)8-barrel fold that is conserved as the catalytic domain in the α-amylase family. Three invariant catalytic carboxylic amino acids in the α-amylase family are also found in GTSase at positions Asp241, Glu269 and Asp460 in the catalytic domain. The shape of the catalytic cavity and the pocket size at the bottom of the cavity correspond to the intramolecular transglycosylation mechanism proposed from previous enzymatic studies.

Crystal structure of tyrosine and phenylalanine hydroxylase catalytic domain

1997 ◽  
Vol 67 (1-4) ◽  
pp. 313 ◽  
Author(s):  
R.C. Stevens ◽  
K.G. Goodwill ◽  
C. Sabatier ◽  
F. Fussetti
Keyword(s):  
Crystal Structure ◽  
Catalytic Domain ◽  
Phenylalanine Hydroxylase

scholarly journals Structural basis of sialidase in complex with geranylated flavonoids as potent natural inhibitors

2014 ◽  
Vol 70 (5) ◽  
pp. 1357-1365 ◽  
Author(s):  
Youngjin Lee ◽  
Young Bae Ryu ◽  
Hyung-Seop Youn ◽  
Jung Keun Cho ◽  
Young Min Kim ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Catalytic Domain ◽  
Enzyme Inhibitor ◽  
Gastrointestinal Diseases ◽  
Structural Basis ◽  
Cellular Interactions ◽  
Inhibitory Effects ◽  
Inhibitor Complex ◽  
Structural Framework ◽  
Natural Inhibitors

Sialidase catalyzes the removal of a terminal sialic acid from glycoconjugates and plays a pivotal role in nutrition, cellular interactions and pathogenesis mediating various infectious diseases including cholera, influenza and sepsis. An array of antiviral sialidase agents have been developed and are commercially available, such as zanamivir and oseltamivir for treating influenza. However, the development of bacterial sialidase inhibitors has been much less successful. Here, natural polyphenolic geranylated flavonoids which show significant inhibitory effects againstCp-NanI, a sialidase fromClostridium perfringens, are reported. This bacterium causes various gastrointestinal diseases. The crystal structure of theCp-NanI catalytic domain in complex with the best inhibitor, diplacone, is also presented. This structure explains how diplacone generates a stable enzyme–inhibitor complex. These results provide a structural framework for understanding the interaction between sialidase and natural flavonoids, which are promising scaffolds on which to discover new anti-sialidase agents.

Crystal Structure and Site-Specific Mutagenesis of Pterin-Bound Human Phenylalanine Hydroxylase†,‡

Biochemistry ◽  
2000 ◽  
Vol 39 (9) ◽  
pp. 2208-2217 ◽  
Author(s):  
Heidi Erlandsen ◽  
Elisa Bjørgo ◽  
Torgeir Flatmark ◽  
Raymond C. Stevens
Keyword(s):  
Crystal Structure ◽  
Phenylalanine Hydroxylase ◽  
Site Specific ◽  
Human Phenylalanine Hydroxylase
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