1os7
From Proteopedia
(New page: 200px<br /><applet load="1os7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1os7, resolution 2.5Å" /> '''Crystal structure of ...) |
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| - | [[Image:1os7.jpg|left|200px]]<br /><applet load="1os7" size=" | + | [[Image:1os7.jpg|left|200px]]<br /><applet load="1os7" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1os7, resolution 2.5Å" /> | caption="1os7, resolution 2.5Å" /> | ||
'''Crystal structure of TauD with iron, alpha-ketoglutarate and Taurine bound at pH 7.5'''<br /> | '''Crystal structure of TauD with iron, alpha-ketoglutarate and Taurine bound at pH 7.5'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The enzymes in the alpha-ketoglutarate (alphaKG) dependent dioxygenase | + | The enzymes in the alpha-ketoglutarate (alphaKG) dependent dioxygenase superfamily represent the largest class of non-heme iron oxidases and have important medical, ecological, and biotechnological roles. One such enzyme, taurine/alpha-ketoglutarate dioxygenase (TauD), catalyzes the conversion of 2-aminoethanesulfonate (taurine) to sulfite and aminoacetaldehyde while decomposing alphaKG to succinate and CO(2). This alphaKG dependent dioxygenase is expressed in Escherichia coli under sulfur starvation conditions and allows the cell to utilize taurine, and other similar sulfonates in the environment, as an alternative sulfur source. In this work, we report the structures of the apo and holo forms of TauD to 1.9 A resolution (R(cryst) = 21.2%, R(free) = 24.9%) and 2.5 A resolution (R(cryst) = 22.5%, R(free) = 27.8%), respectively. The models reported herein provide significant new insight into the substrate orientations at the active site and the conformational changes that are induced upon taurine binding. Furthermore, analysis of our crystallographic data coupled with reanalysis of the crystallographic model (resolution = 3.0 A, R(cryst) = 28.1, R(free) = 32.0) presented by Elkins et al. (Biochemistry (2002) 41, 5185-5192) reveals an alternative oligomeric arrangement for the enzyme that is consistent with the conserved primary and secondary structure elements of other alphaKG dependent dioxygenases. |
==About this Structure== | ==About this Structure== | ||
| - | 1OS7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with FE2, TAU and AKG as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Taurine_dioxygenase Taurine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.17 1.14.11.17] Full crystallographic information is available from [http:// | + | 1OS7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=FE2:'>FE2</scene>, <scene name='pdbligand=TAU:'>TAU</scene> and <scene name='pdbligand=AKG:'>AKG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Taurine_dioxygenase Taurine dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.11.17 1.14.11.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OS7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Taurine dioxygenase]] | [[Category: Taurine dioxygenase]] | ||
| - | [[Category: Brien, J | + | [[Category: Brien, J R.O.]] |
| - | [[Category: Dillard, B | + | [[Category: Dillard, B D.]] |
| - | [[Category: Lanzilotta, W | + | [[Category: Lanzilotta, W N.]] |
| - | [[Category: Schuller, D | + | [[Category: Schuller, D J.]] |
| - | [[Category: Yang, V | + | [[Category: Yang, V S.]] |
[[Category: AKG]] | [[Category: AKG]] | ||
[[Category: FE2]] | [[Category: FE2]] | ||
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[[Category: taurine]] | [[Category: taurine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:03 2008'' |
Revision as of 12:21, 21 February 2008
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Crystal structure of TauD with iron, alpha-ketoglutarate and Taurine bound at pH 7.5
Overview
The enzymes in the alpha-ketoglutarate (alphaKG) dependent dioxygenase superfamily represent the largest class of non-heme iron oxidases and have important medical, ecological, and biotechnological roles. One such enzyme, taurine/alpha-ketoglutarate dioxygenase (TauD), catalyzes the conversion of 2-aminoethanesulfonate (taurine) to sulfite and aminoacetaldehyde while decomposing alphaKG to succinate and CO(2). This alphaKG dependent dioxygenase is expressed in Escherichia coli under sulfur starvation conditions and allows the cell to utilize taurine, and other similar sulfonates in the environment, as an alternative sulfur source. In this work, we report the structures of the apo and holo forms of TauD to 1.9 A resolution (R(cryst) = 21.2%, R(free) = 24.9%) and 2.5 A resolution (R(cryst) = 22.5%, R(free) = 27.8%), respectively. The models reported herein provide significant new insight into the substrate orientations at the active site and the conformational changes that are induced upon taurine binding. Furthermore, analysis of our crystallographic data coupled with reanalysis of the crystallographic model (resolution = 3.0 A, R(cryst) = 28.1, R(free) = 32.0) presented by Elkins et al. (Biochemistry (2002) 41, 5185-5192) reveals an alternative oligomeric arrangement for the enzyme that is consistent with the conserved primary and secondary structure elements of other alphaKG dependent dioxygenases.
About this Structure
1OS7 is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Taurine dioxygenase, with EC number 1.14.11.17 Full crystallographic information is available from OCA.
Reference
Substrate-induced conformational changes in Escherichia coli taurine/alpha-ketoglutarate dioxygenase and insight into the oligomeric structure., O'Brien JR, Schuller DJ, Yang VS, Dillard BD, Lanzilotta WN, Biochemistry. 2003 May 20;42(19):5547-54. PMID:12741810
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