View source for 1fuy


==CRYSTAL STRUCTURE OF BETAA169L/BETAC170W DOUBLE MUTANT OF TRYPTOPHAN SYNTHASE COMPLEXED WITH 5-FLUORO-INDOLE-PROPANOL PHOSPHATE==
<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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FUY FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qop|1qop]], [[1a50|1a50]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fuy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fuy OCA], [http://pdbe.org/1fuy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fuy RCSB], [http://www.ebi.ac.uk/pdbsum/1fuy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fuy ProSAT]</span></td></tr>
</table>
== Function ==
[[http://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. [[http://www.uniprot.org/uniprot/TRPB_SALTY TRPB_SALTY]] The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. 
== 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].
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== Publication Abstract from PubMed ==
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.

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:11034989<ref>PMID:11034989</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 1fuy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Tryptophan synthase]]
[[Category: Schlichting, I]]
[[Category: Weyand, M]]
[[Category: Carbon-oxygen lyase]]
[[Category: Lyase]]
[[Category: Pyridoxal phosphate]]
[[Category: Tryptophan biosynthesis]]