1tyg

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:42, 14 February 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1tyg.jpg|left|200px]]
 
-
{{Structure
+
==Structure of the thiazole synthase/ThiS complex==
-
|PDB= 1tyg |SIZE=350|CAPTION= <scene name='initialview01'>1tyg</scene>, resolution 3.15&Aring;
+
<StructureSection load='1tyg' size='340' side='right'caption='[[1tyg]], [[Resolution|resolution]] 3.15&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
+
<table><tr><td colspan='2'>[[1tyg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TYG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TYG FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.15&#8491;</td></tr>
-
|GENE= thiG,BSU11690 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-
|DOMAIN=
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1tyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tyg OCA], [https://pdbe.org/1tyg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tyg RCSB], [https://www.ebi.ac.uk/pdbsum/1tyg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tyg ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tyg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tyg OCA], [http://www.ebi.ac.uk/pdbsum/1tyg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tyg RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/THIS_BACSU THIS_BACSU] Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate.<ref>PMID:15489164</ref>
-
 
+
== Evolutionary Conservation ==
-
'''Structure of the thiazole synthase/ThiS complex'''
+
[[Image:Consurf_key_small.gif|200px|right]]
-
 
+
Check<jmol>
-
 
+
<jmolCheckbox>
-
==Overview==
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ty/1tyg_consurf.spt"</scriptWhenChecked>
-
Thiazole synthase is the key enzyme involved in the formation of the thiazole moiety of thiamin pyrophosphate. We have determined the structure of this enzyme in complex with ThiS, the sulfur carrier protein, at 3.15 A resolution. Thiazole synthase is a tetramer with 222 symmetry. The monomer is a (betaalpha)(8) barrel with similarities to the aldolase class 1 and flavin mononucleotide dependent oxidoreductase and phosphate binding superfamilies. The sulfur carrier protein (ThiS) is a compact protein with a fold similar to that of ubiquitin. The structure allowed us to model the substrate, deoxy-D-xylulose 5-phosphate (DXP), in the active site. This model identified Glu98 and Asp182 as new active site residues likely to be involved in the catalysis of thiazole formation. The function of these residues was probed by mutagenesis experiments, which confirmed that both residues are essential for thiazole formation and identified Asp182 as the base involved in the deprotonation at C3 of the thiazole synthase DXP imine. Comparison of the ThiS binding surface to the surface of ubiquitin identified a conserved hydrophobic patch of unknown function on ubiquitin that may be involved in complex formation between ubiquitin and one of its binding partners.
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
 
+
<text>to colour the structure by Evolutionary Conservation</text>
-
==About this Structure==
+
</jmolCheckbox>
-
1TYG is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TYG OCA].
+
</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=1tyg ConSurf].
-
 
+
<div style="clear:both"></div>
-
==Reference==
+
== References ==
-
Thiamin biosynthesis in Bacillus subtilis: structure of the thiazole synthase/sulfur carrier protein complex., Settembre EC, Dorrestein PC, Zhai H, Chatterjee A, McLafferty FW, Begley TP, Ealick SE, Biochemistry. 2004 Sep 21;43(37):11647-57. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15362849 15362849]
+
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
-
[[Category: Protein complex]]
+
[[Category: Large Structures]]
-
[[Category: Begley, T P.]]
+
[[Category: Begley TP]]
-
[[Category: Chatterjee, A.]]
+
[[Category: Chatterjee A]]
-
[[Category: Dorrestein, P C.]]
+
[[Category: Dorrestein PC]]
-
[[Category: Ealick, S E.]]
+
[[Category: Ealick SE]]
-
[[Category: McLafferty, F W.]]
+
[[Category: McLafferty FW]]
-
[[Category: Settembre, E C.]]
+
[[Category: Settembre EC]]
-
[[Category: Zhai, H.]]
+
[[Category: Zhai H]]
-
[[Category: alpha beta barrel]]
+
-
[[Category: protein-protein complex]]
+
-
[[Category: thig]]
+
-
[[Category: these]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:02:49 2008''
+

Current revision

Structure of the thiazole synthase/ThiS complex

PDB ID 1tyg

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools