1ude: Difference between revisions

New page: left|200px<br /><applet load="1ude" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ude, resolution 2.66Å" /> '''Crystal structure of...
 
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[[Image:1ude.jpg|left|200px]]<br /><applet load="1ude" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1ude.jpg|left|200px]]<br /><applet load="1ude" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1ude, resolution 2.66&Aring;" />
caption="1ude, resolution 2.66&Aring;" />
'''Crystal structure of the Inorganic pyrophosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3'''<br />
'''Crystal structure of the Inorganic pyrophosphatase from the hyperthermophilic archaeon Pyrococcus horikoshii OT3'''<br />


==Overview==
==Overview==
A homolog to the eubacteria inorganic pyrophosphatase (PPase, EC 3.6.1.1), was found in the genome of the hyperthermophilic archaeon Pyrococcus, horikoshii. This inorganic pyrophosphatase (Pho-PPase) grows optimally at, 88 degrees C. To understand the structural basis for the thermostability, of Pho-PPase, we have determined the crystal structure to 2.66 A, resolution. The crystallographic asymmetric unit contains three monomers, related by approximate threefold symmetry, and a hexamer is built up by, twofold crystallographic symmetry. The main-chain fold of Pho-PPase is, almost identical to that of the known crystal structure of the model from, Sulfolobus acidocaldarius. A detailed comparison of the crystal structure, of Pho-PPase with related structures from S. acidocaldarius, Thermus, thermophilus, and Escherichia coli shows significant differences that may, account for the difference in their thermostabilities. A reduction in, thermolabile residues, additional aromatic residues, and more intimate, association between subunits all contribute to the larger thermophilicity, of Pho-PPase. In particular, deletions in two loops surrounding the active, site help to stabilize its conformation, while ion-pair networks unique to, Pho-PPase are located in the active site and near the C-terminus. The, identification of structural features that make PPases more adaptable to, extreme temperature should prove helpful for future biotechnology, applications.
A homolog to the eubacteria inorganic pyrophosphatase (PPase, EC 3.6.1.1) was found in the genome of the hyperthermophilic archaeon Pyrococcus horikoshii. This inorganic pyrophosphatase (Pho-PPase) grows optimally at 88 degrees C. To understand the structural basis for the thermostability of Pho-PPase, we have determined the crystal structure to 2.66 A resolution. The crystallographic asymmetric unit contains three monomers related by approximate threefold symmetry, and a hexamer is built up by twofold crystallographic symmetry. The main-chain fold of Pho-PPase is almost identical to that of the known crystal structure of the model from Sulfolobus acidocaldarius. A detailed comparison of the crystal structure of Pho-PPase with related structures from S. acidocaldarius, Thermus thermophilus, and Escherichia coli shows significant differences that may account for the difference in their thermostabilities. A reduction in thermolabile residues, additional aromatic residues, and more intimate association between subunits all contribute to the larger thermophilicity of Pho-PPase. In particular, deletions in two loops surrounding the active site help to stabilize its conformation, while ion-pair networks unique to Pho-PPase are located in the active site and near the C-terminus. The identification of structural features that make PPases more adaptable to extreme temperature should prove helpful for future biotechnology applications.


==About this Structure==
==About this Structure==
1UDE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Active as [http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UDE OCA].  
1UDE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii]. Active as [http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UDE OCA].  


==Reference==
==Reference==
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[[Category: inorganic pyrophosphatase x-ray crystallographic analysis]]
[[Category: inorganic pyrophosphatase x-ray crystallographic analysis]]


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