1wq5: Difference between revisions

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New page: left|200px<br /><applet load="1wq5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wq5, resolution 2.30Å" /> '''Crystal structure of...
 
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[[Image:1wq5.gif|left|200px]]<br /><applet load="1wq5" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1wq5, resolution 2.30&Aring;" />
'''Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli'''<br />


==Overview==
==Crystal structure of tryptophan synthase alpha-subunit from Escherichia coli==
When the tryptophan synthase alpha- and beta(2)-subunits combine to form, the alpha(2)beta(2)-complex, the enzymatic activity of each subunit is, stimulated by 1-2 orders of magnitude. To elucidate the structural basis, of this mutual activation, it is necessary to determine the structures of, the alpha- and beta-subunits alone and together with the, alpha(2)beta(2)-complex. The crystal structures of the tryptophan synthase, alpha(2)beta(2)-complex from Salmonella typhimurium, (Stalpha(2)beta(2)-complex) have already been reported. However, the, structures of the subunit alone from mesophiles have not yet been, determined. The structure of the tryptophan synthase alpha-subunit alone, from Escherichia coli (Ecalpha-subunit) was determined by an X-ray, crystallographic analysis at 2.3 A, which is the first report on the, subunits alone from the mesophiles. The biggest difference between the, structures of the Ecalpha-subunit alone and the alpha-subunit in the, Stalpha(2)beta(2)-complex (Stalpha-subunit) was as follows. Helix 2' in, the Stalpha-subunit, including an active site residue (Asp60), was changed, to a flexible loop in the Ecalpha-subunit alone. The conversion of the, helix to a loop resulted in the collapse of the correct active site, conformation. This region is also an important part for the mutual, activation in the Stalpha(2)beta(2)-complex and interaction with the, beta-subunit. These results suggest that the formation of helix 2'that is, essential for the stimulation of the enzymatic activity of the, alpha-subunit is constructed by the induced-fit mode involved in, conformational changes upon interaction between the alpha- and, beta-subunits. This also confirms the prediction of the conformational, changes based on the thermodynamic analysis for the association between, the alpha- and beta-subunits.
<StructureSection load='1wq5' size='340' side='right'caption='[[1wq5]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wq5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WQ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WQ5 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]] 2.3&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1wq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wq5 OCA], [https://pdbe.org/1wq5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wq5 RCSB], [https://www.ebi.ac.uk/pdbsum/1wq5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wq5 ProSAT], [https://www.topsan.org/Proteins/RSGI/1wq5 TOPSAN]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRPA_ECOLI TRPA_ECOLI] 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/wq/1wq5_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=1wq5 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1WQ5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with SO4 and GOL 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=1WQ5 OCA].
*[[Tryptophan synthase 3D structures|Tryptophan synthase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Conformational changes in the alpha-subunit coupled to binding of the beta 2-subunit of tryptophan synthase from Escherichia coli: crystal structure of the tryptophan synthase alpha-subunit alone., Nishio K, Morimoto Y, Ishizuka M, Ogasahara K, Tsukihara T, Yutani K, Biochemistry. 2005 Feb 1;44(4):1184-92. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15667212 15667212]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Tryptophan synthase]]
[[Category: Ishizuka M]]
[[Category: Ishizuka, M.]]
[[Category: Morimoto Y]]
[[Category: Morimoto, Y.]]
[[Category: Nishio K]]
[[Category: Nishio, K.]]
[[Category: Ogasahara K]]
[[Category: Ogasahara, K.]]
[[Category: Tsukihara T]]
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
[[Category: Yutani K]]
[[Category: Tsukihara, T.]]
[[Category: Yutani, K.]]
[[Category: GOL]]
[[Category: SO4]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: structural genomics]]
[[Category: tryptophan]]
[[Category: tryptophan synthase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 05:36:04 2007''

Latest revision as of 16:33, 13 March 2024

Crystal structure of tryptophan synthase alpha-subunit from Escherichia coliCrystal structure of tryptophan synthase alpha-subunit from Escherichia coli

Structural highlights

1wq5 is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

TRPA_ECOLI 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

1wq5, resolution 2.30Å

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