1k7f
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1k7f.jpg|left|200px]] | + | [[Image:1k7f.jpg|left|200px]] |
| - | + | ||
| - | '''CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH N-[1H-INDOL-3-YL-ACETYL]VALINE ACID''' | + | {{Structure |
| + | |PDB= 1k7f |SIZE=350|CAPTION= <scene name='initialview01'>1k7f</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=IAV:N-[1H-INDOL-3-YL-ACETYL]VALINE+ACID'>IAV</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> | ||
| + | |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] | ||
| + | |GENE= TRPA/TRPB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=602 Salmonella typhimurium]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH N-[1H-INDOL-3-YL-ACETYL]VALINE ACID''' | ||
| + | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1K7F is a [ | + | 1K7F 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=1K7F OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structures of a new class of allosteric effectors complexed to tryptophan synthase., Weyand M, Schlichting I, Marabotti A, Mozzarelli A, J Biol Chem. 2002 Mar 22;277(12):10647-52. Epub 2001 Dec 26. PMID:[http:// | + | Crystal structures of a new class of allosteric effectors complexed to tryptophan synthase., Weyand M, Schlichting I, Marabotti A, Mozzarelli A, J Biol Chem. 2002 Mar 22;277(12):10647-52. Epub 2001 Dec 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11756456 11756456] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Salmonella typhimurium]] | [[Category: Salmonella typhimurium]] | ||
| Line 24: | Line 33: | ||
[[Category: tryptophan biosynthesis]] | [[Category: tryptophan biosynthesis]] | ||
| - | ''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 12:13:35 2008'' |
Revision as of 10:13, 20 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | TRPA/TRPB (Salmonella typhimurium) | ||||||
| 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 N-[1H-INDOL-3-YL-ACETYL]VALINE ACID
Overview
Tryptophan synthase is a bifunctional alpha(2)beta(2) complex catalyzing the last two steps of l-tryptophan biosynthesis. The natural substrates of the alpha-subunit indole- 3-glycerolphosphate and glyceraldehyde-3-phosphate, and the substrate analogs indole-3-propanolphosphate and dl-alpha-glycerol-3-phosphate are allosteric effectors of the beta-subunit activity. It has been shown recently, that the indole-3-acetyl amino acids indole-3-acetylglycine and indole-3-acetyl-l-aspartic acid are both alpha-subunit inhibitors and beta-subunit allosteric effectors, whereas indole-3-acetyl-l-valine is only an alpha-subunit inhibitor (Marabotti, A., Cozzini, P., and Mozzarelli, A. (2000) Biochim. Biophys. Acta 1476, 287-299). The crystal structures of tryptophan synthase complexed with indole-3-acetylglycine and indole-3-acetyl-l-aspartic acid show that both ligands bind to the active site such that the carboxylate moiety is positioned similarly as the phosphate group of the natural substrates. As a consequence, the residues of the alpha-active site that interact with the ligands are the same as observed in the indole 3-glycerolphosphate-enzyme complex. Ligand binding leads to closure of loop alphaL6 of the alpha-subunit, a key structural element of intersubunit communication. This is in keeping with the allosteric role played by these compounds. The structure of the enzyme complex with indole-3-acetyl-l-valine is quite different. Due to the hydrophobic lateral chain, this molecule adopts a new orientation in the alpha-active site. In this case, closure of loop alphaL6 is no longer observed, in agreement with its functioning only as an inhibitor of the alpha-subunit reaction.
About this Structure
1K7F is a Protein complex structure of sequences from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Crystal structures of a new class of allosteric effectors complexed to tryptophan synthase., Weyand M, Schlichting I, Marabotti A, Mozzarelli A, J Biol Chem. 2002 Mar 22;277(12):10647-52. Epub 2001 Dec 26. PMID:11756456
Page seeded by OCA on Thu Mar 20 12:13:35 2008
