1exk: Difference between revisions
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'''SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.''' | {{Structure | ||
|PDB= 1exk |SIZE=350|CAPTION= <scene name='initialview01'>1exk</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1EXK is a [ | 1EXK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXK OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10891270 10891270] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc-binding motif]] | [[Category: zinc-binding motif]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:01:37 2008'' | ||
Revision as of 09:01, 20 March 2008
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| Ligands: | ZN | ||||||||||||
| 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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