1kfb

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[[Image:1kfb.jpg|left|200px]]
[[Image:1kfb.jpg|left|200px]]
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{{Structure
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|PDB= 1kfb |SIZE=350|CAPTION= <scene name='initialview01'>1kfb</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1kfb", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=IGP:INDOLE-3-GLYCEROL+PHOSPHATE'>IGP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5&#39;-PHOSPHATE'>PLP</scene>
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{{STRUCTURE_1kfb| PDB=1kfb | SCENE= }}
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|RELATEDENTRY=[[1k8x|1K8X]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfb OCA], [http://www.ebi.ac.uk/pdbsum/1kfb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kfb RCSB]</span>
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'''CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM WITH Indole Glycerol Phosphate'''
'''CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM WITH Indole Glycerol Phosphate'''
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[[Category: Siedel, R.]]
[[Category: Siedel, R.]]
[[Category: Weyand, M.]]
[[Category: Weyand, M.]]
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[[Category: helix]]
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[[Category: Helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:40:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:47:50 2008''
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Revision as of 19:40, 2 May 2008

Template:STRUCTURE 1kfb

CRYSTAL STRUCTURE OF ALPHAT183V MUTANT OF TRYPTOPHAN SYNTHASE FROM SALMONELLA TYPHIMURIUM WITH Indole Glycerol Phosphate


Overview

The catalytic activity and substrate channeling of the pyridoxal 5'-phosphate-dependent tryptophan synthase alpha(2)beta(2) complex is regulated by allosteric interactions that modulate the switching of the enzyme between open, low activity and closed, high activity states during the catalytic cycle. The highly conserved alphaThr183 residue is part of loop alphaL6 and is located next to the alpha-active site and forms part of the alpha-beta subunit interface. The role of the interactions of alphaThr183 in alpha-site catalysis and allosteric regulation was investigated by analyzing the kinetics and crystal structures of the isosteric mutant alphaThr183Val. The mutant displays strongly impaired allosteric alpha-beta communication, and the catalytic activity of the alpha-reaction is reduced one hundred fold, whereas the beta-activity is not affected. The structural work establishes that the basis for the missing inter-subunit signaling is the lack of loop alphaL6 closure even in the presence of the alpha-subunit ligands, 3-indolyl-D-glycerol 3'-phosphate, or 3-indolylpropanol 3'-phosphate. The structural basis for the reduced alpha-activity has its origins in the missing hydrogen bond between alphaThr183 and the catalytic residue, alphaAsp60.

About this Structure

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

Reference

On the role of alphaThr183 in the allosteric regulation and catalytic mechanism of tryptophan synthase., Kulik V, Weyand M, Seidel R, Niks D, Arac D, Dunn MF, Schlichting I, J Mol Biol. 2002 Dec 6;324(4):677-90. PMID:12460570 Page seeded by OCA on Fri May 2 22:40:32 2008

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