1exk
From Proteopedia
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|PDB= 1exk |SIZE=350|CAPTION= <scene name='initialview01'>1exk</scene> | |PDB= 1exk |SIZE=350|CAPTION= <scene name='initialview01'>1exk</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <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=1exk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exk OCA], [http://www.ebi.ac.uk/pdbsum/1exk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1exk RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Wright, P E.]] | [[Category: Wright, P E.]] | ||
[[Category: Zhang, O.]] | [[Category: Zhang, O.]] | ||
| - | [[Category: ZN]] | ||
[[Category: cxxcxgxg]] | [[Category: cxxcxgxg]] | ||
[[Category: extended beta-hairpin]] | [[Category: extended beta-hairpin]] | ||
[[Category: zinc-binding motif]] | [[Category: zinc-binding motif]] | ||
| - | ''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 20:11:36 2008'' |
Revision as of 17:11, 30 March 2008
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.
Overview
The solution structure of the cysteine-rich (CR) domain of Escherichia coli DnaJ has been solved by NMR methods. The structure of a 79 residue CR domain construct shows a novel fold with an overall V-shaped extended beta-hairpin topology. The CR domain is characterized by four C-X-X-C-X-G-X-G sequence motifs that bind two zinc ions. Residues in these two zinc modules show strong similarities in the grouping of resonances in the (15)N-(1)H HSQC spectrum and display pseudo-symmetry of the motifs in the calculated structures. The conformation of the cysteine residues coordinated to the zinc ion resembles that of the rubredoxin-knuckle, but there are significant differences in hydrogen bonding patterns in the two motifs. Zinc (15)N-(1)H HSQC titrations indicate that the fold of the isolated DnaJ CR domain is zinc-dependent and that one zinc module folds before the other. The C-X-X-C-X-G-X-G sequence motif is highly conserved in CR domains from a wide variety of species. The three-dimensional structure of the E. coli CR domain indicates that this sequence conservation is likely to result in a conserved structural motif.
About this Structure
1EXK is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure of the cysteine-rich domain of the Escherichia coli chaperone protein DnaJ., Martinez-Yamout M, Legge GB, Zhang O, Wright PE, Dyson HJ, J Mol Biol. 2000 Jul 21;300(4):805-18. PMID:10891270
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