1zud
From Proteopedia
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|PDB= 1zud |SIZE=350|CAPTION= <scene name='initialview01'>1zud</scene>, resolution 1.98Å | |PDB= 1zud |SIZE=350|CAPTION= <scene name='initialview01'>1zud</scene>, resolution 1.98Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zud OCA], [http://www.ebi.ac.uk/pdbsum/1zud PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zud RCSB]</span> | ||
}} | }} | ||
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[[Category: Ealick, S E.]] | [[Category: Ealick, S E.]] | ||
[[Category: Lehmann, C.]] | [[Category: Lehmann, C.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: NA]] | ||
| - | [[Category: ZN]] | ||
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
[[Category: thiamin]] | [[Category: thiamin]] | ||
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[[Category: these]] | [[Category: these]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:41:44 2008'' |
Revision as of 22:41, 30 March 2008
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| , resolution 1.98Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of ThiS-ThiF protein complex
Overview
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
1ZUD is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
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