Crystal structure of bullfrog M ferritin at 2.8 Å resolution: analysis of subunit interactions and the binuclear metal center

1999 ◽  
Vol 4 (3) ◽  
pp. 243-256 ◽  
Author(s):  
Y. Ha ◽  
Dashuang Shi ◽  
George W. Small ◽  
Elizabeth C. Theil ◽  
N. M. Allewell
Keyword(s):  
Crystal Structure ◽  
Metal Center ◽  
Subunit Interactions ◽  
Resolution Analysis ◽  
Binuclear Metal

scholarly journals Crystal structures of a ZIP zinc transporter reveal a binuclear metal center in the transport pathway

2017 ◽  
Vol 3 (8) ◽  
pp. e1700344 ◽  
Author(s):  
Tuo Zhang ◽  
Jian Liu ◽  
Matthias Fellner ◽  
Chi Zhang ◽  
Dexin Sui ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Zinc Transporter ◽  
Metal Center ◽  
Transport Pathway ◽  
Binuclear Metal

A combinatorial library for the binuclear metal center of bacterial phosphotriesterase

1997 ◽  
Vol 29 (4) ◽  
pp. 553-561 ◽  
Author(s):  
Linette M. Watkins ◽  
Jane M. Kuo ◽  
Misty Chen-Goodspeed ◽  
Frank M. Raushel
Keyword(s):  
Combinatorial Library ◽  
Metal Center ◽  
Binuclear Metal

scholarly journals Biochemical and Structural Insights into Xylan Utilization by the Thermophilic Bacterium Caldanaerobius polysaccharolyticus

2012 ◽  
Vol 287 (42) ◽  
pp. 34946-34960 ◽  
Author(s):  
Yejun Han ◽  
Vinayak Agarwal ◽  
Dylan Dodd ◽  
Jason Kim ◽  
Brian Bae ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Gene Cluster ◽  
Plant Cell Wall ◽  
Hydrolytic Enzymes ◽  
Thermophilic Bacterium ◽  
Pentose Phosphate ◽  
Structural Basis ◽  
Resolution Analysis ◽  
Calorimetric Studies ◽  
Hydrolysis Of

Hemicellulose is the next most abundant plant cell wall component after cellulose. The abundance of hemicellulose such as xylan suggests that their hydrolysis and conversion to biofuels can improve the economics of bioenergy production. In an effort to understand xylan hydrolysis at high temperatures, we sequenced the genome of the thermophilic bacterium Caldanaerobius polysaccharolyticus. Analysis of the partial genome sequence revealed a gene cluster that contained both hydrolytic enzymes and also enzymes key to the pentose-phosphate pathway. The hydrolytic enzymes in the gene cluster were demonstrated to convert products from a large endoxylanase (Xyn10A) predicted to anchor to the surface of the bacterium. We further use structural and calorimetric studies to demonstrate that the end products of Xyn10A hydrolysis of xylan are recognized and bound by XBP1, a putative solute-binding protein, likely for transport into the cell. The XBP1 protein showed preference for xylo-oligosaccharides as follows: xylotriose > xylobiose > xylotetraose. To elucidate the structural basis for the oligosaccharide preference, we solved the co-crystal structure of XBP1 complexed with xylotriose to a 1.8-Å resolution. Analysis of the biochemical data in the context of the co-crystal structure reveals the molecular underpinnings of oligosaccharide length specificity.

Protonation of the Binuclear Metal Center within the Active Site of Phosphotriesterase†

Biochemistry ◽  
2005 ◽  
Vol 44 (33) ◽  
pp. 11005-11013 ◽  
Author(s):  
Cynthia R. Samples ◽  
Timothy Howard ◽  
Frank M. Raushel ◽  
Victoria J. DeRose
Keyword(s):  
Active Site ◽  
Metal Center ◽  
Binuclear Metal

scholarly journals Structure of Diethyl Phosphate Bound to the Binuclear Metal Center of Phosphotriesterase†‡

Biochemistry ◽  
2008 ◽  
Vol 47 (36) ◽  
pp. 9497-9504 ◽  
Author(s):  
Jungwook Kim ◽  
Ping-Chuan Tsai ◽  
Shi-Lu Chen ◽  
Fahmi Himo ◽  
Steven C. Almo ◽  
...  
Keyword(s):  
Metal Center ◽  
Diethyl Phosphate ◽  
Binuclear Metal

Overexpression and Purification of Human Calcineurin α fromEscherichia coliand Assessment of Catalytic Functions of Residues Surrounding the Binuclear Metal Center†

Biochemistry ◽  
1997 ◽  
Vol 36 (16) ◽  
pp. 4934-4942 ◽  
Author(s):  
Angelo Mondragon ◽  
Eric C. Griffith ◽  
Luo Sun ◽  
Fei Xiong ◽  
Christopher Armstrong ◽  
...  
Keyword(s):  
Metal Center ◽  
Binuclear Metal ◽  
Catalytic Functions

scholarly journals Asymmetric functions of a binuclear metal center within the transport pathway of a human zinc transporter ZIP4

2019 ◽  
Vol 34 (1) ◽  
pp. 237-247 ◽  
Author(s):  
Tuo Zhang ◽  
Dexin Sui ◽  
Chi Zhang ◽  
Logan Cole ◽  
Jian Hu
Keyword(s):  
Zinc Transporter ◽  
Metal Center ◽  
Transport Pathway ◽  
Binuclear Metal
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