2p3v

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[[Image:2p3v.gif|left|200px]]<br /><applet load="2p3v" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2p3v.gif|left|200px]]
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caption="2p3v, resolution 2.4&Aring;" />
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'''Thermotoga maritima IMPase TM1415'''<br />
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{{Structure
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|PDB= 2p3v |SIZE=350|CAPTION= <scene name='initialview01'>2p3v</scene>, resolution 2.4&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SRT:S,R MESO-TARTARIC ACID'>SRT</scene>
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|ACTIVITY= [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]
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|GENE= suhB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
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}}
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'''Thermotoga maritima IMPase TM1415'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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2P3V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P3V OCA].
==Reference==
==Reference==
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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 May;274(10):2461-9. Epub 2007 Apr 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17419729 17419729]
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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 May;274(10):2461-9. Epub 2007 Apr 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17419729 17419729]
[[Category: Inositol-phosphate phosphatase]]
[[Category: Inositol-phosphate phosphatase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: phosphatase]]
[[Category: phosphatase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:25:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:08:16 2008''

Revision as of 16:08, 20 March 2008


PDB ID 2p3v

Drag the structure with the mouse to rotate
, resolution 2.4Å
Ligands:
Gene: suhB (Thermotoga maritima)
Activity: Inositol-phosphate phosphatase, with EC number 3.1.3.25
Coordinates: save as pdb, mmCIF, xml



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. 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 May;274(10):2461-9. Epub 2007 Apr 10. PMID:17419729

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