2oqx

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[[Image:2oqx.gif|left|200px]]<br /><applet load="2oqx" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2oqx.gif|left|200px]]
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caption="2oqx, resolution 1.900&Aring;" />
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'''Crystal Structure of the apo form of E. coli tryptophanase at 1.9 A resolution'''<br />
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{{Structure
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|PDB= 2oqx |SIZE=350|CAPTION= <scene name='initialview01'>2oqx</scene>, resolution 1.900&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'>EPE</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Tryptophanase Tryptophanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.1 4.1.99.1]
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|GENE=
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}}
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'''Crystal Structure of the apo form of E. coli tryptophanase at 1.9 A resolution'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2OQX 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=CL:'>CL</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=EPE:'>EPE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Tryptophanase Tryptophanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.1 4.1.99.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQX OCA].
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2OQX 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=2OQX OCA].
==Reference==
==Reference==
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The structure of apo tryptophanase from Escherichia coli reveals a wide-open conformation., Tsesin N, Kogan A, Gdalevsky GY, Himanen JP, Cohen-Luria R, Parola AH, Goldgur Y, Almog O, Acta Crystallogr D Biol Crystallogr. 2007 Sep;63(Pt 9):969-74. Epub 2007, Aug 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17704565 17704565]
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The structure of apo tryptophanase from Escherichia coli reveals a wide-open conformation., Tsesin N, Kogan A, Gdalevsky GY, Himanen JP, Cohen-Luria R, Parola AH, Goldgur Y, Almog O, Acta Crystallogr D Biol Crystallogr. 2007 Sep;63(Pt 9):969-74. Epub 2007, Aug 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17704565 17704565]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: tryptophan catabolism]]
[[Category: tryptophan catabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:21:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:03:19 2008''

Revision as of 16:03, 20 March 2008

Image:2oqx.gif


PDB ID 2oqx

Drag the structure with the mouse to rotate
, resolution 1.900Å
Ligands: , and
Activity: Tryptophanase, with EC number 4.1.99.1
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the apo form of E. coli tryptophanase at 1.9 A resolution


Overview

The crystal structure of apo tryptophanase from Escherichia coli (space group F222, unit-cell parameters a = 118.4, b = 120.1, c = 171.2 A) was determined at 1.9 A resolution using the molecular-replacement method and refined to an R factor of 20.3% (R(free) = 23.2%). The structure revealed a significant shift in the relative orientation of the domains compared with both the holo form of Proteus vulgaris tryptophanase and with another crystal structure of apo E. coli tryptophanase, reflecting the internal flexibility of the molecule. Domain shifts were previously observed in tryptophanase and in the closely related enzyme tyrosine phenol-lyase, with the holo form found in an open conformation and the apo form in either an open or a closed conformation. Here, a wide-open conformation of the apo form of tryptophanase is reported. A conformational change is also observed in loop 297-303. The structure contains a hydrated Mg(2+) at the cation-binding site and a Cl(-) ion at the subunit interface. The enzyme activity depends on the nature of the bound cation, with smaller ions serving as inhibitors. It is hypothesized that this effect arises from variations of the coordination geometry of the bound cation.

About this Structure

2OQX is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The structure of apo tryptophanase from Escherichia coli reveals a wide-open conformation., Tsesin N, Kogan A, Gdalevsky GY, Himanen JP, Cohen-Luria R, Parola AH, Goldgur Y, Almog O, Acta Crystallogr D Biol Crystallogr. 2007 Sep;63(Pt 9):969-74. Epub 2007, Aug 17. PMID:17704565

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