2ot2: Difference between revisions

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==Overview==

Escherichia coli HypC plays an important role in the maturation process of, the pre-maturated HycE, the large subunit of hydrogenase 3. It serves as, an iron transfer as well as a chaperone protein during the maturation, process of pre-HycE, and interacts with both HypD and HycE. The N-terminal, cysteine residue of HypC plays a key role in the protein-protein, interactions. Here, we present the three-dimensional structure of E. coli, HypC, the first solution structure of HupF/HypC family. Our result, demonstrates that E. coli HypC consists of a typical OB-fold beta-barrel, with two C-terminal helixes. Sequence alignment and structural comparison, reveal that the hydrophobic region on the surface of E. coli HypC, as well, as the highly flexible C-terminal helixes, may involve in the interactions, of E. coli HypC with other proteins.

Escherichia coli HypC plays an important role in the maturation process of the pre-maturated HycE, the large subunit of hydrogenase 3. It serves as an iron transfer as well as a chaperone protein during the maturation process of pre-HycE, and interacts with both HypD and HycE. The N-terminal cysteine residue of HypC plays a key role in the protein-protein interactions. Here, we present the three-dimensional structure of E. coli HypC, the first solution structure of HupF/HypC family. Our result demonstrates that E. coli HypC consists of a typical OB-fold beta-barrel with two C-terminal helixes. Sequence alignment and structural comparison reveal that the hydrophobic region on the surface of E. coli HypC, as well as the highly flexible C-terminal helixes, may involve in the interactions of E. coli HypC with other proteins.

==About this Structure==

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[[Category: chaperone]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jan 23 13~~:46:15 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:22:15 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Escherichia coli HypC plays an important role in the maturation process of, the pre-maturated HycE, the large subunit of hydrogenase 3. It serves as, an iron transfer as well as a chaperone protein during the maturation, process of pre-HycE, and interacts with both HypD and HycE. The N-terminal, cysteine residue of HypC plays a key role in the protein-protein, interactions. Here, we present the three-dimensional structure of E. coli, HypC, the first solution structure of HupF/HypC family. Our result, demonstrates that E. coli HypC consists of a typical OB-fold beta-barrel, with two C-terminal helixes. Sequence alignment and structural comparison, reveal that the hydrophobic region on the surface of E. coli HypC, as well, as the highly flexible C-terminal helixes, may involve in the interactions, of E. coli HypC with other proteins.
+Escherichia coli HypC plays an important role in the maturation process of the pre-maturated HycE, the large subunit of hydrogenase 3. It serves as an iron transfer as well as a chaperone protein during the maturation process of pre-HycE, and interacts with both HypD and HycE. The N-terminal cysteine residue of HypC plays a key role in the protein-protein interactions. Here, we present the three-dimensional structure of E. coli HypC, the first solution structure of HupF/HypC family. Our result demonstrates that E. coli HypC consists of a typical OB-fold beta-barrel with two C-terminal helixes. Sequence alignment and structural comparison reveal that the hydrophobic region on the surface of E. coli HypC, as well as the highly flexible C-terminal helixes, may involve in the interactions of E. coli HypC with other proteins.
 ==About this Structure==
@@ Line 18: / Line 18: @@
 [[Category: chaperone]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:46:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:22:15 2008''