2p3v
From Proteopedia
(New page: 200px<br /><applet load="2p3v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2p3v, resolution 2.4Å" /> '''Thermotoga maritima I...) |
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| - | [[Image:2p3v.gif|left|200px]]<br /><applet load="2p3v" size=" | + | [[Image:2p3v.gif|left|200px]]<br /><applet load="2p3v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2p3v, resolution 2.4Å" /> | caption="2p3v, resolution 2.4Å" /> | ||
'''Thermotoga maritima IMPase TM1415'''<br /> | '''Thermotoga maritima IMPase TM1415'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2P3V 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 SRT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inositol-phosphate_phosphatase Inositol-phosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.25 3.1.3.25] Full crystallographic information is available from [http:// | + | 2P3V 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=SRT:'>SRT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inositol-phosphate_phosphatase Inositol-phosphate phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.25 3.1.3.25] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P3V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: phosphatase]] | [[Category: phosphatase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:15:25 2008'' |
Revision as of 13:15, 23 January 2008
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Thermotoga maritima IMPase TM1415
Overview
The structure of the first tetrameric inositol monophosphatase (IMPase), has been solved. This enzyme, from the eubacterium Thermotoga maritima, similarly to its archaeal homologs exhibits dual specificity with both, IMPase and fructose-1,6-bisphosphatase activities. The tetrameric, structure of this unregulated enzyme is similar, in its quaternary, assembly, to the allosterically regulated tetramer of, fructose-1,6-bisphosphatase. The individual dimers are similar to the, human IMPase. Additionally, the structures of two crystal forms of IMPase, show significant differences. In the first crystal form, the tetrameric, structure is symmetrical, with the active site loop in each subunit folded, into a beta-hairpin conformation. The second form is asymmetrical and, shows an unusual structural change. Two of the subunits have the active, site loop folded into a beta-hairpin structure, whereas in the remaining, two subunits the same loop adopts an alpha-helical conformation.
About this Structure
2P3V is a Single protein structure of sequence from Thermotoga maritima with as ligand. Active as Inositol-phosphate phosphatase, with EC number 3.1.3.25 Full crystallographic information is available from OCA.
Reference
Crystal structure of the tetrameric inositol 1-phosphate phosphatase (TM1415) from the hyperthermophile, Thermotoga maritima., Stieglitz KA, Roberts MF, Li W, Stec B, FEBS J. 2007 Apr 10;. PMID:17419729
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