1zb1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1zb1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zb1, resolution 1.95&Aring;" /> '''Structure basis for ...)
Line 1: Line 1:
-
[[Image:1zb1.gif|left|200px]]<br /><applet load="1zb1" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1zb1.gif|left|200px]]<br /><applet load="1zb1" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1zb1, resolution 1.95&Aring;" />
caption="1zb1, resolution 1.95&Aring;" />
'''Structure basis for endosomal targeting by the Bro1 domain'''<br />
'''Structure basis for endosomal targeting by the Bro1 domain'''<br />
==Overview==
==Overview==
-
Proteins delivered to the lysosome or the yeast vacuole via late endosomes, are sorted by the ESCRT complexes and by associated proteins, including, Alix and its yeast homolog Bro1. Alix, Bro1, and several other late, endosomal proteins share a conserved 160 residue Bro1 domain whose, boundaries, structure, and function have not been characterized. The, crystal structure of the Bro1 domain of Bro1 reveals a folded core of 367, residues. The extended Bro1 domain is necessary and sufficient for binding, to the ESCRT-III subunit Snf7 and for the recruitment of Bro1 to late, endosomes. The structure resembles a boomerang with its concave face, filled in and contains a triple tetratricopeptide repeat domain as a, substructure. Snf7 binds to a conserved hydrophobic patch on Bro1 that is, required for protein complex formation and for the protein-sorting, function of Bro1. These results define a conserved mechanism whereby Bro1, domain-containing proteins are targeted to endosomes by Snf7 and its, orthologs.
+
Proteins delivered to the lysosome or the yeast vacuole via late endosomes are sorted by the ESCRT complexes and by associated proteins, including Alix and its yeast homolog Bro1. Alix, Bro1, and several other late endosomal proteins share a conserved 160 residue Bro1 domain whose boundaries, structure, and function have not been characterized. The crystal structure of the Bro1 domain of Bro1 reveals a folded core of 367 residues. The extended Bro1 domain is necessary and sufficient for binding to the ESCRT-III subunit Snf7 and for the recruitment of Bro1 to late endosomes. The structure resembles a boomerang with its concave face filled in and contains a triple tetratricopeptide repeat domain as a substructure. Snf7 binds to a conserved hydrophobic patch on Bro1 that is required for protein complex formation and for the protein-sorting function of Bro1. These results define a conserved mechanism whereby Bro1 domain-containing proteins are targeted to endosomes by Snf7 and its orthologs.
==About this Structure==
==About this Structure==
-
1ZB1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZB1 OCA].
+
1ZB1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZB1 OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Beach, B.M.]]
+
[[Category: Beach, B M.]]
[[Category: Hierro, A.]]
[[Category: Hierro, A.]]
-
[[Category: Hurley, J.H.]]
+
[[Category: Hurley, J H.]]
[[Category: Kim, J.]]
[[Category: Kim, J.]]
[[Category: Odorizzi, G.]]
[[Category: Odorizzi, G.]]
Line 25: Line 25:
[[Category: trafficking]]
[[Category: trafficking]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:21:23 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:52 2008''

Revision as of 14:14, 21 February 2008


1zb1, resolution 1.95Å

Drag the structure with the mouse to rotate

Structure basis for endosomal targeting by the Bro1 domain

Overview

Proteins delivered to the lysosome or the yeast vacuole via late endosomes are sorted by the ESCRT complexes and by associated proteins, including Alix and its yeast homolog Bro1. Alix, Bro1, and several other late endosomal proteins share a conserved 160 residue Bro1 domain whose boundaries, structure, and function have not been characterized. The crystal structure of the Bro1 domain of Bro1 reveals a folded core of 367 residues. The extended Bro1 domain is necessary and sufficient for binding to the ESCRT-III subunit Snf7 and for the recruitment of Bro1 to late endosomes. The structure resembles a boomerang with its concave face filled in and contains a triple tetratricopeptide repeat domain as a substructure. Snf7 binds to a conserved hydrophobic patch on Bro1 that is required for protein complex formation and for the protein-sorting function of Bro1. These results define a conserved mechanism whereby Bro1 domain-containing proteins are targeted to endosomes by Snf7 and its orthologs.

About this Structure

1ZB1 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural basis for endosomal targeting by the Bro1 domain., Kim J, Sitaraman S, Hierro A, Beach BM, Odorizzi G, Hurley JH, Dev Cell. 2005 Jun;8(6):937-47. PMID:15935782

Page seeded by OCA on Thu Feb 21 16:13:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools