1qop

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[[Image:1qop.gif|left|200px]]<br /><applet load="1qop" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qop.gif|left|200px]]
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caption="1qop, resolution 1.4&Aring;" />
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'''CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH INDOLE PROPANOL PHOSPHATE'''<br />
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{{Structure
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|PDB= 1qop |SIZE=350|CAPTION= <scene name='initialview01'>1qop</scene>, resolution 1.4&Aring;
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|SITE= <scene name='pdbsite=IPL:Substrate+Analog+Bound+To+The+Alpha+Activ'>IPL</scene>, <scene name='pdbsite=NA:Na+Binding+Site+For+Chain+B'>NA</scene> and <scene name='pdbsite=PLP:Plp+Binding+Site+For+Chain+B'>PLP</scene>
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|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=IPL:INDOLE-3-PROPANOL+PHOSPHATE'>IPL</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH INDOLE PROPANOL PHOSPHATE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1QOP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=IPL:'>IPL</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] Known structural/functional Sites: <scene name='pdbsite=IPL:Substrate+Analog+Bound+To+The+Alpha+Activ'>IPL</scene>, <scene name='pdbsite=NA:Na+Binding+Site+For+Chain+B'>NA</scene> and <scene name='pdbsite=PLP:Plp+Binding+Site+For+Chain+B'>PLP</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOP OCA].
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1QOP is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOP OCA].
==Reference==
==Reference==
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Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate., Weyand M, Schlichting I, Biochemistry. 1999 Dec 14;38(50):16469-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10600108 10600108]
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Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate., Weyand M, Schlichting I, Biochemistry. 1999 Dec 14;38(50):16469-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10600108 10600108]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Salmonella typhimurium]]
[[Category: Salmonella typhimurium]]
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[[Category: tryptophan biosynthesis]]
[[Category: tryptophan biosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:40:34 2008''

Revision as of 11:40, 20 March 2008


PDB ID 1qop

Drag the structure with the mouse to rotate
, resolution 1.4Å
Sites: , and
Ligands: , and
Activity: Tryptophan synthase, with EC number 4.2.1.20
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH INDOLE PROPANOL PHOSPHATE


Overview

We used freeze trapping to stabilize the Michaelis complex of wild-type tryptophan synthase and the alpha-subunit substrate indole-3-glycerol phosphate (IGP) and determined its structure to 1. 8 A resolution. In addition, we determined the 1.4 A resolution structure of the complex with indole-3-propanole phosphate (IPP), a noncleavable IGP analogue. The interaction of the 3'-hydroxyl of IGP with the catalytic alphaGlu49 leads to a twisting of the propane chain and to a repositioning of the indole ring compared to IPP. Concomitantly, the catalytic alphaAsp60 rotates resulting in a translocation of the COMM domain [betaGly102-betaGly189, for definition see Schneider et al. (1998) Biochemistry 37, 5394-5406] in a direction opposite to the one in the IPP complex. This results in loss of the allosteric sodium ion bound at the beta-subunit and an opening of the beta-active site, thereby making the cofactor pyridoxal 5'-phosphate (PLP) accessible to solvent and thus serine binding. These findings form the structural basis for the information transfer from the alpha- to the beta-subunit and may explain the affinity increase of the beta-active site for serine upon IGP binding.

About this Structure

1QOP is a Protein complex structure of sequences from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

Crystal structure of wild-type tryptophan synthase complexed with the natural substrate indole-3-glycerol phosphate., Weyand M, Schlichting I, Biochemistry. 1999 Dec 14;38(50):16469-80. PMID:10600108

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