1g7d: Difference between revisions

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[[Image:1g7d.gif|left|200px]]<br /><applet load="1g7d" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1g7d.gif|left|200px]]<br /><applet load="1g7d" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1g7d" />

'''NMR STRUCTURE OF ERP29 C-DOMAIN'''<br />

==Overview==

BACKGROUND: ERp29 is a ubiquitously expressed rat endoplasmic reticulum, (ER) protein conserved in mammalian species. Fold predictions suggest the, presence of a thioredoxin-like domain homologous to the a domain of human, protein disulfide isomerase (PDI) and a helical domain similar to the, C-terminal domain of P5-like PDIs. As ERp29 lacks the double-cysteine, motif essential for PDI redox activity, it is suggested to play a role in, protein maturation and/or secretion related to the chaperone function of, PDI. ERp29 self-associates into 51 kDa dimers and also higher oligomers., RESULTS: 3D structures of the N- and C-terminal domains determined by NMR, spectroscopy confirmed the thioredoxin fold for the N-terminal domain and, yielded a novel all-helical fold for the C-terminal domain. Studies of the, full-length protein revealed a short, flexible linker between the two, domains, homodimerization by the N-terminal domain, and the presence of, interaction sites for the formation of higher molecular weight oligomers., A gadolinium-based relaxation agent is shown to present a sensitive tool, for the identification of macromolecular interfaces by NMR. CONCLUSIONS:, ERp29 is the first eukaryotic PDI-related protein for which the structures, of all domains have been determined. Furthermore, an experimental model of, the full-length protein and its association states was established. It is, the first example of a protein where the thioredoxin fold was found to act, as a specific homodimerization module, without covalent linkages or, supporting interactions by further domains. A homodimerization module, similar as in ERp29 may also be present in homodimeric human PDI.

BACKGROUND: ERp29 is a ubiquitously expressed rat endoplasmic reticulum (ER) protein conserved in mammalian species. Fold predictions suggest the presence of a thioredoxin-like domain homologous to the a domain of human protein disulfide isomerase (PDI) and a helical domain similar to the C-terminal domain of P5-like PDIs. As ERp29 lacks the double-cysteine motif essential for PDI redox activity, it is suggested to play a role in protein maturation and/or secretion related to the chaperone function of PDI. ERp29 self-associates into 51 kDa dimers and also higher oligomers. RESULTS: 3D structures of the N- and C-terminal domains determined by NMR spectroscopy confirmed the thioredoxin fold for the N-terminal domain and yielded a novel all-helical fold for the C-terminal domain. Studies of the full-length protein revealed a short, flexible linker between the two domains, homodimerization by the N-terminal domain, and the presence of interaction sites for the formation of higher molecular weight oligomers. A gadolinium-based relaxation agent is shown to present a sensitive tool for the identification of macromolecular interfaces by NMR. CONCLUSIONS: ERp29 is the first eukaryotic PDI-related protein for which the structures of all domains have been determined. Furthermore, an experimental model of the full-length protein and its association states was established. It is the first example of a protein where the thioredoxin fold was found to act as a specific homodimerization module, without covalent linkages or supporting interactions by further domains. A homodimerization module similar as in ERp29 may also be present in homodimeric human PDI.

==About this Structure==

1G7D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1G7D OCA].

1G7D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7D OCA].

==Reference==

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[[Category: alpha helical protein]]

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@@ Line 1: / Line 1: @@
-[[Image:1g7d.gif|left|200px]]<br /><applet load="1g7d" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1g7d.gif|left|200px]]<br /><applet load="1g7d" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1g7d" />
 '''NMR STRUCTURE OF ERP29 C-DOMAIN'''<br />
 ==Overview==
-BACKGROUND: ERp29 is a ubiquitously expressed rat endoplasmic reticulum, (ER) protein conserved in mammalian species. Fold predictions suggest the, presence of a thioredoxin-like domain homologous to the a domain of human, protein disulfide isomerase (PDI) and a helical domain similar to the, C-terminal domain of P5-like PDIs. As ERp29 lacks the double-cysteine, motif essential for PDI redox activity, it is suggested to play a role in, protein maturation and/or secretion related to the chaperone function of, PDI. ERp29 self-associates into 51 kDa dimers and also higher oligomers., RESULTS: 3D structures of the N- and C-terminal domains determined by NMR, spectroscopy confirmed the thioredoxin fold for the N-terminal domain and, yielded a novel all-helical fold for the C-terminal domain. Studies of the, full-length protein revealed a short, flexible linker between the two, domains, homodimerization by the N-terminal domain, and the presence of, interaction sites for the formation of higher molecular weight oligomers., A gadolinium-based relaxation agent is shown to present a sensitive tool, for the identification of macromolecular interfaces by NMR. CONCLUSIONS:, ERp29 is the first eukaryotic PDI-related protein for which the structures, of all domains have been determined. Furthermore, an experimental model of, the full-length protein and its association states was established. It is, the first example of a protein where the thioredoxin fold was found to act, as a specific homodimerization module, without covalent linkages or, supporting interactions by further domains. A homodimerization module, similar as in ERp29 may also be present in homodimeric human PDI.
+BACKGROUND: ERp29 is a ubiquitously expressed rat endoplasmic reticulum (ER) protein conserved in mammalian species. Fold predictions suggest the presence of a thioredoxin-like domain homologous to the a domain of human protein disulfide isomerase (PDI) and a helical domain similar to the C-terminal domain of P5-like PDIs. As ERp29 lacks the double-cysteine motif essential for PDI redox activity, it is suggested to play a role in protein maturation and/or secretion related to the chaperone function of PDI. ERp29 self-associates into 51 kDa dimers and also higher oligomers. RESULTS: 3D structures of the N- and C-terminal domains determined by NMR spectroscopy confirmed the thioredoxin fold for the N-terminal domain and yielded a novel all-helical fold for the C-terminal domain. Studies of the full-length protein revealed a short, flexible linker between the two domains, homodimerization by the N-terminal domain, and the presence of interaction sites for the formation of higher molecular weight oligomers. A gadolinium-based relaxation agent is shown to present a sensitive tool for the identification of macromolecular interfaces by NMR. CONCLUSIONS: ERp29 is the first eukaryotic PDI-related protein for which the structures of all domains have been determined. Furthermore, an experimental model of the full-length protein and its association states was established. It is the first example of a protein where the thioredoxin fold was found to act as a specific homodimerization module, without covalent linkages or supporting interactions by further domains. A homodimerization module similar as in ERp29 may also be present in homodimeric human PDI.
 ==About this Structure==
-G7D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G7D OCA].
+G7D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7D OCA].
 ==Reference==
@@ Line 21: / Line 21: @@
 [[Category: alpha helical protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:46:50 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:56 2008''