1zud

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1zud" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zud, resolution 1.98&Aring;" /> '''Structure of ThiS-Th...)
Current revision (07:14, 23 August 2023) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1zud.gif|left|200px]]<br /><applet load="1zud" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1zud, resolution 1.98&Aring;" />
 
-
'''Structure of ThiS-ThiF protein complex'''<br />
 
-
==Overview==
+
==Structure of ThiS-ThiF protein complex==
-
We have determined the crystal structure of the Escherichia coli ThiS-ThiF, protein complex at 2.0 A resolution. ThiS and ThiF are bacterial proteins, involved in the synthesis of the thiazole moiety of thiamin. ThiF, catalyzes the adenylation of the carboxy terminus of ThiS and the, subsequent displacement of AMP catalyzed by ThiI-persulfide to give a, ThiS-ThiI acyl disulfide. Disulfide interchange, involving Cys184 on ThiF, then generates the ThiS-ThiF acyl disulfide, which functions as the sulfur, donor for thiazole formation. ThiS is a small 7.2 kDa protein that, structurally resembles ubiquitin and the molybdopterin biosynthetic, protein MoaD. ThiF is a 27 kDa protein with distinct sequence and, structural similarity to the ubiquitin activating enzyme E1 and the, molybdopterin biosynthetic protein MoeB. The ThiF-ThiS structure clarifies, the mechanism of the sulfur transfer chemistry involved in thiazole, biosynthesis.
+
<StructureSection load='1zud' size='340' side='right'caption='[[1zud]], [[Resolution|resolution]] 1.98&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1zud]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZUD 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]] 1.98&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1zud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zud OCA], [https://pdbe.org/1zud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zud RCSB], [https://www.ebi.ac.uk/pdbsum/1zud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zud ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/THIF_ECOLI THIF_ECOLI] Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS.
 +
== 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/zu/1zud_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=1zud ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
We have determined the crystal structure of the Escherichia coli ThiS-ThiF protein complex at 2.0 A resolution. ThiS and ThiF are bacterial proteins involved in the synthesis of the thiazole moiety of thiamin. ThiF catalyzes the adenylation of the carboxy terminus of ThiS and the subsequent displacement of AMP catalyzed by ThiI-persulfide to give a ThiS-ThiI acyl disulfide. Disulfide interchange, involving Cys184 on ThiF, then generates the ThiS-ThiF acyl disulfide, which functions as the sulfur donor for thiazole formation. ThiS is a small 7.2 kDa protein that structurally resembles ubiquitin and the molybdopterin biosynthetic protein MoaD. ThiF is a 27 kDa protein with distinct sequence and structural similarity to the ubiquitin activating enzyme E1 and the molybdopterin biosynthetic protein MoeB. The ThiF-ThiS structure clarifies the mechanism of the sulfur transfer chemistry involved in thiazole biosynthesis.
-
==About this Structure==
+
Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis.,Lehmann C, Begley TP, Ealick SE Biochemistry. 2006 Jan 10;45(1):11-9. PMID:16388576<ref>PMID:16388576</ref>
-
1ZUD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN, CA and NA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZUD OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis., Lehmann C, Begley TP, Ealick SE, Biochemistry. 2006 Jan 10;45(1):11-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16388576 16388576]
+
</div>
-
[[Category: Escherichia coli]]
+
<div class="pdbe-citations 1zud" style="background-color:#fffaf0;"></div>
-
[[Category: Protein complex]]
+
== References ==
-
[[Category: Ealick, S.E.]]
+
<references/>
-
[[Category: Lehmann, C.]]
+
__TOC__
-
[[Category: CA]]
+
</StructureSection>
-
[[Category: NA]]
+
[[Category: Escherichia coli K-12]]
-
[[Category: ZN]]
+
[[Category: Large Structures]]
-
[[Category: protein-protein complex]]
+
[[Category: Ealick SE]]
-
[[Category: thiamin]]
+
[[Category: Lehmann C]]
-
[[Category: thiazole]]
+
-
[[Category: thif]]
+
-
[[Category: this]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:39:56 2007''
+

Current revision

Structure of ThiS-ThiF protein complex

PDB ID 1zud

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/1zud"
Personal tools