1ons
From Proteopedia
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|PDB= 1ons |SIZE=350|CAPTION= <scene name='initialview01'>1ons</scene>, resolution 2.2Å | |PDB= 1ons |SIZE=350|CAPTION= <scene name='initialview01'>1ons</scene>, resolution 2.2Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= HCHA OR B1967 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= HCHA OR B1967 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ons FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ons OCA], [http://www.ebi.ac.uk/pdbsum/1ons PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ons RCSB]</span> | ||
}} | }} | ||
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[[Category: Fox, R O.]] | [[Category: Fox, R O.]] | ||
[[Category: Zhao, Y.]] | [[Category: Zhao, Y.]] | ||
| - | [[Category: ZN]] | ||
[[Category: chaperone]] | [[Category: chaperone]] | ||
[[Category: heat shock protein]] | [[Category: heat shock protein]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:48:02 2008'' |
Revision as of 19:48, 30 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | HCHA OR B1967 (Escherichia coli) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Escherichia coli heat shock protein YedU
Overview
The mRNA of Escherichia coli yedU gene is induced 31-fold upon heat shock. The 31-kD YedU protein, also calls Hsp31, is highly conserved in several human pathogens and has chaperone activity. We solved the crystal structure of YedU at 2.2 A resolution. YedU monomer has an alpha/beta/alpha sandwich domain and a small alpha/beta domain. YedU is a dimer in solution, and its crystal structure indicates that a significant amount of surface area is buried upon dimerization. There is an extended hydrophobic patch that crosses the dimer interface on the surface of the protein. This hydrophobic patch is likely the substrate-binding site responsible for the chaperone activity. The structure also reveals a potential protease-like catalytic triad composed of Cys184, His185, and Asp213, although no enzymatic activity could be identified. YedU coordinates a metal ion using His85, His122, and Glu90. This 2-His-1-carboxylate motif is present in carboxypeptidase A (a zinc enzyme), and a number of dioxygenases and hydroxylases that utilize iron as a cofactor, suggesting another potential function for YedU.
About this Structure
1ONS is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The crystal structure of Escherichia coli heat shock protein YedU reveals three potential catalytic active sites., Zhao Y, Liu D, Kaluarachchi WD, Bellamy HD, White MA, Fox RO, Protein Sci. 2003 Oct;12(10):2303-11. PMID:14500888
Page seeded by OCA on Sun Mar 30 22:48:02 2008
Categories: Escherichia coli | Single protein | Fox, R O. | Zhao, Y. | Chaperone | Heat shock protein | Hsp31 | Protease | Stress response | Yedu | Zinc
