1b9b: Difference between revisions
New page: left|200px<br /><applet load="1b9b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b9b, resolution 2.85Å" /> '''TRIOSEPHOSPHATE ISOM... |
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[[Image:1b9b.jpg|left|200px]]<br /><applet load="1b9b" size=" | [[Image:1b9b.jpg|left|200px]]<br /><applet load="1b9b" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1b9b, resolution 2.85Å" /> | caption="1b9b, resolution 2.85Å" /> | ||
'''TRIOSEPHOSPHATE ISOMERASE OF THERMOTOGA MARITIMA'''<br /> | '''TRIOSEPHOSPHATE ISOMERASE OF THERMOTOGA MARITIMA'''<br /> | ||
==Overview== | ==Overview== | ||
The molecular mechanisms that evolution has been employing to adapt to | The molecular mechanisms that evolution has been employing to adapt to environmental temperatures are poorly understood. To gain some further insight into this subject we solved the crystal structure of triosephosphate isomerase (TIM) from the hyperthermophilic bacterium Thermotoga maritima (TmTIM). The enzyme is a tetramer, assembled as a dimer of dimers, suggesting that the tetrameric wild-type phosphoglycerate kinase PGK-TIM fusion protein consists of a core of two TIM dimers covalently linked to 4 PGK units. The crystal structure of TmTIM represents the most thermostable TIM presently known in its 3D-structure. It adds to a series of nine known TIM structures from a wide variety of organisms, spanning the range from psychrophiles to hyperthermophiles. Several properties believed to be involved in the adaptation to different temperatures were calculated and compared for all ten structures. No sequence preferences, correlated with thermal stability, were apparent from the amino acid composition or from the analysis of the loops and secondary structure elements of the ten TIMs. A common feature for both psychrophilic and T. maritima TIM is the large number of salt bridges compared with the number found in mesophilic TIMs. In the two thermophilic TIMs, the highest amount of accessible hydrophobic surface is buried during the folding and assembly process. | ||
==About this Structure== | ==About this Structure== | ||
1B9B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] Full crystallographic information is available from [http:// | 1B9B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9B OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Triose-phosphate isomerase]] | [[Category: Triose-phosphate isomerase]] | ||
[[Category: Maes, D.]] | [[Category: Maes, D.]] | ||
[[Category: Wierenga, R | [[Category: Wierenga, R K.]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
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[[Category: thermotoga maritima]] | [[Category: thermotoga maritima]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:52:52 2008'' |