2trs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:24, 21 February 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2trs.jpg|left|200px]]<br /><applet load="2trs" size="350" color="white" frame="true" align="right" spinBox="true"
 
-
caption="2trs, resolution 2.04&Aring;" />
 
-
'''CRYSTAL STRUCTURES OF MUTANT (BETAK87T) TRYPTOPHAN SYNTHASE ALPHA2 BETA2 COMPLEX WITH LIGANDS BOUND TO THE ACTIVE SITES OF THE ALPHA AND BETA SUBUNITS REVEAL LIGAND-INDUCED CONFORMATIONAL CHANGES'''<br />
 
-
==Overview==
+
==CRYSTAL STRUCTURES OF MUTANT (BETAK87T) TRYPTOPHAN SYNTHASE ALPHA2 BETA2 COMPLEX WITH LIGANDS BOUND TO THE ACTIVE SITES OF THE ALPHA AND BETA SUBUNITS REVEAL LIGAND-INDUCED CONFORMATIONAL CHANGES==
-
Three-dimensional structures are reported for a mutant (betaK87T), tryptophan synthase alpha2beta2 complex with either the substrate L-serine, (betaK87T-Ser) or product L-tryptophan (betaK87T-Trp) at the active site, of the beta-subunit, in which both amino acids form external aldimines, with the coenzyme, pyridoxal phosphate. We also present structures with, L-serine bound to the beta site and either alpha-glycerol 3-phosphate, (betaK87T-Ser-GP) or indole-3-propanol phosphate (betaK87T-Ser-IPP) bound, to the active site of the alpha-subunit. The results further identify the, substrate and product binding sites in each subunit and provide insight, into conformational changes that occur upon formation of these complexes., The two structures having ligands at the active sites of both alpha- and, beta-subunits reveal an important new feature, the ordering of, alpha-subunit loop 6 (residues 179-187). Closure of loop 6 isolates the, active site of the alpha-subunit from solvent and results in interaction, between alphaThr183 and the catalytic residue alphaAsp60. Other, conformational differences between the wild type and these two mutant, structures include a rigid-body rotation of the alpha-subunit of, approximately 5 degrees relative to the beta-subunit and large movements, of part of the beta-subunit (residues 93-189) toward the rest of the, beta-subunit. Much smaller differences are observed in the betaK87T-Ser, structure. Remarkably, binding of tryptophan to the beta active site, results in conformational changes very similar to those observed in the, betaK87T-Ser-GP and betaK87T-Ser-IPP structures, with exception of the, disordered alpha-subunit loop 6. These large-scale changes, the closure of, loop 6, and the movements of a small number of side chains in the, alpha-beta interaction site provide a structural base for interpreting the, allosteric properties of tryptophan synthase.
+
<StructureSection load='2trs' size='340' side='right'caption='[[2trs]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[2trs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2TRS FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.04&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPL:INDOLE-3-PROPANOL+PHOSPHATE'>IPL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLS:[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-SERINE'>PLS</scene></td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2trs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2trs OCA], [https://pdbe.org/2trs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2trs RCSB], [https://www.ebi.ac.uk/pdbsum/2trs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2trs ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/TRPA_SALTY TRPA_SALTY] The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/tr/2trs_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2trs ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
2TRS 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=PLS:'>PLS</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=S1:Substrate+Analog+Bound+To+The+Alpha+Active+Site'>S1</scene> and <scene name='pdbsite=S2:Reaction+Intermediate+Bound+To+The+Beta+Active+Site'>S2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2TRS OCA].
+
*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes., Rhee S, Parris KD, Hyde CC, Ahmed SA, Miles EW, Davies DR, Biochemistry. 1997 Jun 24;36(25):7664-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9201907 9201907]
+
[[Category: Large Structures]]
-
[[Category: Protein complex]]
+
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
-
[[Category: Salmonella typhimurium]]
+
[[Category: Ahmed SA]]
-
[[Category: Tryptophan synthase]]
+
[[Category: Davies DR]]
-
[[Category: Ahmed, S.A.]]
+
[[Category: Hyde CC]]
-
[[Category: Davies, D.R.]]
+
[[Category: Miles EW]]
-
[[Category: Hyde, C.C.]]
+
[[Category: Parris KD]]
-
[[Category: Miles, E.W.]]
+
[[Category: Rhee S]]
-
[[Category: Parris, K.D.]]
+
-
[[Category: Rhee, S.]]
+
-
[[Category: IPL]]
+
-
[[Category: NA]]
+
-
[[Category: PLS]]
+
-
[[Category: carbon-oxygen lyase]]
+
-
[[Category: lyase]]
+
-
[[Category: pyridoxal phosphate]]
+
-
[[Category: tryptophan biosynthesis]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:46:56 2008''
+

Current revision

CRYSTAL STRUCTURES OF MUTANT (BETAK87T) TRYPTOPHAN SYNTHASE ALPHA2 BETA2 COMPLEX WITH LIGANDS BOUND TO THE ACTIVE SITES OF THE ALPHA AND BETA SUBUNITS REVEAL LIGAND-INDUCED CONFORMATIONAL CHANGES

PDB ID 2trs

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2trs"
Personal tools