1fuy: Difference between revisions

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New page: left|200px<br /><applet load="1fuy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fuy, resolution 2.25Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1fuy.gif|left|200px]]<br /><applet load="1fuy" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1fuy, resolution 2.25&Aring;" />
'''CRYSTAL STRUCTURE OF BETAA169L/BETAC170W DOUBLE MUTANT OF TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUORO-INDOLE-PROPANOL PHOSPHATE'''<br />


==Overview==
==CRYSTAL STRUCTURE OF BETAA169L/BETAC170W DOUBLE MUTANT OF TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUORO-INDOLE-PROPANOL PHOSPHATE==
We determined the 2.25 A resolution crystal structure of the, betaA169L/betaC170W mutant form of the tryptophan synthase alpha(2)beta(2), complex from Salmonella typhimurium complexed with the alpha-active site, substrate analogue 5-fluoro-indole-propanol-phosphate to identify the, structural basis for the changed kinetic properties of the mutant, (Anderson, K. S., Kim, A. Y., Quillen, J. M., Sayers, E., Yang, X. J., and, Miles, E. W. (1995) J. Biol. Chem. 270, 29936-29944). Comparison with the, wild-type enzyme showed that the betaTrp(170) side chain occludes the, tunnel connecting the alpha- and beta-active sites, explaining the, accumulation of the intermediate indole during a single enzyme turnover., To prevent a steric clash between betaLeu(169) and betaGly(135), located, in the beta-sheet of the COMM (communication) domain, (betaGly(102)-betaGly(189)), the latter reorganizes. The changed COMM, domain conformation results in a loss of the hydrogen bonding networks, between the alpha- and beta-active sites, explaining the poor activation, of the alpha-reaction upon formation of the aminoacrylate complex at the, beta-active site. The 100-fold reduced affinity for serine seems to result, from a movement of betaAsp(305) away from the beta-active site so that it, cannot interact with the hydroxyl group of a pyridoxal phosphate-bound, serine. The proposed structural dissection of the effects of each single, mutation in the betaA169L/betaC170W mutant would explain the very, different kinetics of this mutant and betaC170F.
<StructureSection load='1fuy' size='340' side='right'caption='[[1fuy]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fuy]] 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=1FUY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUY 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]] 2.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FIP:5-FLUOROINDOLE+PROPANOL+PHOSPHATE'>FIP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [https://pdbe.org/1fuy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [https://www.ebi.ac.uk/pdbsum/1fuy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fuy 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/fu/1fuy_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=1fuy ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1FUY 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, FIP 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FUY OCA].
*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase., Weyand M, Schlichting I, J Biol Chem. 2000 Dec 29;275(52):41058-63. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11034989 11034989]
[[Category: Large Structures]]
[[Category: Protein complex]]
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium]]
[[Category: Salmonella typhimurium]]
[[Category: Schlichting I]]
[[Category: Tryptophan synthase]]
[[Category: Weyand M]]
[[Category: Schlichting, I.]]
[[Category: Weyand, M.]]
[[Category: FIP]]
[[Category: NA]]
[[Category: PLP]]
[[Category: carbon-oxygen lyase]]
[[Category: lyase]]
[[Category: pyridoxal phosphate]]
[[Category: tryptophan biosynthesis]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:19:21 2007''

Latest revision as of 14:16, 27 March 2024

CRYSTAL STRUCTURE OF BETAA169L/BETAC170W DOUBLE MUTANT OF TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUORO-INDOLE-PROPANOL PHOSPHATECRYSTAL STRUCTURE OF BETAA169L/BETAC170W DOUBLE MUTANT OF TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUORO-INDOLE-PROPANOL PHOSPHATE

Structural highlights

1fuy is a 2 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TRPA_SALTY The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1fuy, resolution 2.25Å

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