1qop
From Proteopedia
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| - | [[Image:1qop.gif|left|200px]]<br /><applet load="1qop" size=" | + | [[Image:1qop.gif|left|200px]]<br /><applet load="1qop" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qop, resolution 1.4Å" /> | caption="1qop, resolution 1.4Å" /> | ||
'''CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH INDOLE PROPANOL PHOSPHATE'''<br /> | '''CRYSTAL STRUCTURE OF WILD-TYPE TRYPTOPHAN SYNTHASE COMPLEXED WITH INDOLE PROPANOL PHOSPHATE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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 NA, IPL and PLP 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: tryptophan biosynthesis]] | [[Category: tryptophan biosynthesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:01:28 2008'' |
Revision as of 08:01, 3 February 2008
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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 with , and as ligands. Active as Tryptophan synthase, with EC number 4.2.1.20 Known structural/functional Sites: , and . 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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