1otj
From Proteopedia
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| - | [[Image:1otj.jpg|left|200px]] | + | [[Image:1otj.jpg|left|200px]] |
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| - | '''Crystal structure of APO (iron-free) TauD''' | + | {{Structure |
| + | |PDB= 1otj |SIZE=350|CAPTION= <scene name='initialview01'>1otj</scene>, resolution 1.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=TAU:2-AMINOETHANESULFONIC ACID'>TAU</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of APO (iron-free) TauD''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1OTJ is a [ | + | 1OTJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OTJ OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12741810 12741810] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: taurine]] | [[Category: taurine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:15:28 2008'' |
Revision as of 11:15, 20 March 2008
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| , resolution 1.9Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Taurine dioxygenase, with EC number 1.14.11.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of APO (iron-free) TauD
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
1OTJ is a Single protein structure of sequence from Escherichia coli. 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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