1nwm

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(New page: 200px<br /> <applet load="1nwm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nwm, resolution 2.40&Aring;" /> '''GAT domain of human...)
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'''GAT domain of human GGA1'''<br />
'''GAT domain of human GGA1'''<br />
==Overview==
==Overview==
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The Golgi-associated, gamma-adaptin homologous, ADP-ribosylation factor, (ARF)-interacting proteins (GGAs) are adaptors that sort receptors from, the trans-Golgi network into the endosomallysosomal pathway. The GGAs and, TOM1 (GAT) domains of the GGAs are responsible for their ARF-dependent, localization. The 2.4-A crystal structure of the GAT domain of human GGA1, reveals a three-helix bundle, with a long N-terminal helical extension, that is not conserved in GAT domains that do not bind ARF. The ARF binding, site is located in the N-terminal extension and is separate from the core, three-helix bundle. An unanticipated structural similarity to the, N-terminal domain of syntaxin 1a was discovered, comprising the entire, three-helix bundle. A conserved binding site on helices 2 and 3 of the GAT, domain three-helix bundle is predicted to interact with, coiled-coil-containing proteins. We propose that the GAT domain is, descended from the same ancestor as the syntaxin 1a N-terminal domain, and, that both protein families share a common function in binding coiled-coil, domain proteins.
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The Golgi-associated, gamma-adaptin homologous, ADP-ribosylation factor (ARF)-interacting proteins (GGAs) are adaptors that sort receptors from the trans-Golgi network into the endosomallysosomal pathway. The GGAs and TOM1 (GAT) domains of the GGAs are responsible for their ARF-dependent localization. The 2.4-A crystal structure of the GAT domain of human GGA1 reveals a three-helix bundle, with a long N-terminal helical extension that is not conserved in GAT domains that do not bind ARF. The ARF binding site is located in the N-terminal extension and is separate from the core three-helix bundle. An unanticipated structural similarity to the N-terminal domain of syntaxin 1a was discovered, comprising the entire three-helix bundle. A conserved binding site on helices 2 and 3 of the GAT domain three-helix bundle is predicted to interact with coiled-coil-containing proteins. We propose that the GAT domain is descended from the same ancestor as the syntaxin 1a N-terminal domain, and that both protein families share a common function in binding coiled-coil domain proteins.
==About this Structure==
==About this Structure==
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1NWM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NWM OCA].
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1NWM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NWM OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Hurley, J.H.]]
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[[Category: Hurley, J H.]]
[[Category: Misra, S.]]
[[Category: Misra, S.]]
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[[Category: Saidi, L.F.]]
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[[Category: Saidi, L F.]]
[[Category: Suer, S.]]
[[Category: Suer, S.]]
[[Category: three-alpha helical bundle]]
[[Category: three-alpha helical bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:26:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:55 2008''

Revision as of 12:11, 21 February 2008


1nwm, resolution 2.40Å

Drag the structure with the mouse to rotate

GAT domain of human GGA1

Overview

The Golgi-associated, gamma-adaptin homologous, ADP-ribosylation factor (ARF)-interacting proteins (GGAs) are adaptors that sort receptors from the trans-Golgi network into the endosomallysosomal pathway. The GGAs and TOM1 (GAT) domains of the GGAs are responsible for their ARF-dependent localization. The 2.4-A crystal structure of the GAT domain of human GGA1 reveals a three-helix bundle, with a long N-terminal helical extension that is not conserved in GAT domains that do not bind ARF. The ARF binding site is located in the N-terminal extension and is separate from the core three-helix bundle. An unanticipated structural similarity to the N-terminal domain of syntaxin 1a was discovered, comprising the entire three-helix bundle. A conserved binding site on helices 2 and 3 of the GAT domain three-helix bundle is predicted to interact with coiled-coil-containing proteins. We propose that the GAT domain is descended from the same ancestor as the syntaxin 1a N-terminal domain, and that both protein families share a common function in binding coiled-coil domain proteins.

About this Structure

1NWM is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structure of the GAT domain of human GGA1: a syntaxin amino-terminal domain fold in an endosomal trafficking adaptor., Suer S, Misra S, Saidi LF, Hurley JH, Proc Natl Acad Sci U S A. 2003 Apr 15;100(8):4451-6. Epub 2003 Mar 31. PMID:12668765

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