1exk
From Proteopedia
(New page: 200px<br /><applet load="1exk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1exk" /> '''SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMA...) |
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| - | [[Image:1exk.jpg|left|200px]]<br /><applet load="1exk" size=" | + | [[Image:1exk.jpg|left|200px]]<br /><applet load="1exk" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1exk" /> | caption="1exk" /> | ||
'''SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.'''<br /> | '''SOLUTION STRUCTURE OF THE CYSTEINE-RICH DOMAIN OF THE ESCHERICHIA COLI CHAPERONE PROTEIN DNAJ.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The solution structure of the cysteine-rich (CR) domain of Escherichia | + | 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== | ==About this Structure== | ||
| - | 1EXK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1EXK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dyson, H | + | [[Category: Dyson, H J.]] |
| - | [[Category: Legge, G | + | [[Category: Legge, G B.]] |
[[Category: Martinez-Yamout, M.]] | [[Category: Martinez-Yamout, M.]] | ||
| - | [[Category: Wright, P | + | [[Category: Wright, P E.]] |
[[Category: Zhang, O.]] | [[Category: Zhang, O.]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: zinc-binding motif]] | [[Category: zinc-binding motif]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:32:32 2008'' |
Revision as of 10:32, 21 February 2008
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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 with as ligand. 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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