1z2x: Difference between revisions

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[[Image:1z2x.gif|left|200px]]<br /><applet load="1z2x" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1z2x.gif|left|200px]]<br /><applet load="1z2x" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1z2x, resolution 2.22Å" />

'''Crystal structure of mouse Vps29'''<br />

==Overview==

The retromer complex is responsible for the retrieval of mannose, 6-phosphate receptors from the endosomal system to the Golgi. Here we, present the crystal structure of the mammalian retromer subunit mVps29 and, show that it has structural similarity to divalent metal-containing, phosphoesterases. mVps29 can coordinate metals in a similar manner but has, no detectable phosphoesterase activity in vitro, suggesting a unique, specificity or function. The mVps29 and mVps26 subunits bind independently, to mVps35 and together form a high-affinity heterotrimeric subcomplex., Mutagenesis reveals the structural basis for the interaction of mVps29, with mVps35 and subsequent association with endosomal membranes in vivo. A, conserved hydrophobic surface distinct from the primary Vps35p binding, site mediates assembly of the Vps29p-Vps26p-Vps35p subcomplex with sorting, nexins in yeast, and mutation of either site results in a defect in, retromer-dependent membrane trafficking.

The retromer complex is responsible for the retrieval of mannose 6-phosphate receptors from the endosomal system to the Golgi. Here we present the crystal structure of the mammalian retromer subunit mVps29 and show that it has structural similarity to divalent metal-containing phosphoesterases. mVps29 can coordinate metals in a similar manner but has no detectable phosphoesterase activity in vitro, suggesting a unique specificity or function. The mVps29 and mVps26 subunits bind independently to mVps35 and together form a high-affinity heterotrimeric subcomplex. Mutagenesis reveals the structural basis for the interaction of mVps29 with mVps35 and subsequent association with endosomal membranes in vivo. A conserved hydrophobic surface distinct from the primary Vps35p binding site mediates assembly of the Vps29p-Vps26p-Vps35p subcomplex with sorting nexins in yeast, and mutation of either site results in a defect in retromer-dependent membrane trafficking.

==About this Structure==

1Z2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1Z2X OCA].

1Z2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2X OCA].

==Reference==

Line 13:

[[Category: Mus musculus]]

[[Category: Single protein]]

[[Category: Collins, B.M.]]

[[Category: Collins, B M.]]

[[Category: Owen, D.J.]]

[[Category: Owen, D J.]]

[[Category: Seaman, M.N.J.]]

[[Category: Seaman, M N.J.]]

[[Category: Skinner, C.F.]]

[[Category: Skinner, C F.]]

[[Category: Watson, P.J.]]

[[Category: Watson, P J.]]

[[Category: phosphatase]]

[[Category: retromer]]

[[Category: vps29]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Wed Nov~~ 21 07:12:~~55 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:40 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1z2x.gif|left|200px]]<br /><applet load="1z2x" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1z2x.gif|left|200px]]<br /><applet load="1z2x" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1z2x, resolution 2.22&Aring;" />
 '''Crystal structure of mouse Vps29'''<br />
 ==Overview==
-The retromer complex is responsible for the retrieval of mannose, 6-phosphate receptors from the endosomal system to the Golgi. Here we, present the crystal structure of the mammalian retromer subunit mVps29 and, show that it has structural similarity to divalent metal-containing, phosphoesterases. mVps29 can coordinate metals in a similar manner but has, no detectable phosphoesterase activity in vitro, suggesting a unique, specificity or function. The mVps29 and mVps26 subunits bind independently, to mVps35 and together form a high-affinity heterotrimeric subcomplex., Mutagenesis reveals the structural basis for the interaction of mVps29, with mVps35 and subsequent association with endosomal membranes in vivo. A, conserved hydrophobic surface distinct from the primary Vps35p binding, site mediates assembly of the Vps29p-Vps26p-Vps35p subcomplex with sorting, nexins in yeast, and mutation of either site results in a defect in, retromer-dependent membrane trafficking.
+The retromer complex is responsible for the retrieval of mannose 6-phosphate receptors from the endosomal system to the Golgi. Here we present the crystal structure of the mammalian retromer subunit mVps29 and show that it has structural similarity to divalent metal-containing phosphoesterases. mVps29 can coordinate metals in a similar manner but has no detectable phosphoesterase activity in vitro, suggesting a unique specificity or function. The mVps29 and mVps26 subunits bind independently to mVps35 and together form a high-affinity heterotrimeric subcomplex. Mutagenesis reveals the structural basis for the interaction of mVps29 with mVps35 and subsequent association with endosomal membranes in vivo. A conserved hydrophobic surface distinct from the primary Vps35p binding site mediates assembly of the Vps29p-Vps26p-Vps35p subcomplex with sorting nexins in yeast, and mutation of either site results in a defect in retromer-dependent membrane trafficking.
 ==About this Structure==
-Z2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z2X OCA].
+Z2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z2X OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Mus musculus]]
 [[Category: Single protein]]
-[[Category: Collins, B.M.]]
+[[Category: Collins, B M.]]
-[[Category: Owen, D.J.]]
+[[Category: Owen, D J.]]
-[[Category: Seaman, M.N.J.]]
+[[Category: Seaman, M N.J.]]
-[[Category: Skinner, C.F.]]
+[[Category: Skinner, C F.]]
-[[Category: Watson, P.J.]]
+[[Category: Watson, P J.]]
 [[Category: phosphatase]]
 [[Category: retromer]]
 [[Category: vps29]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:12:55 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:40 2008''