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=" | [[Image:1ude.jpg|left|200px]]<br /><applet load="1ude" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ude, resolution 2.66Å" /> | caption="1ude, resolution 2.66Å" /> | ||
'''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) | 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:// | 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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