1z5w: Difference between revisions

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[[Image:1z5w.gif|left|200px]]<br />

[[Image:1z5w.gif|left|200px]]<br /><applet load="1z5w" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1z5w" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1z5w, resolution 3.00Å" />

'''Crystal Structure of gamma-tubulin bound to GTP'''<br />

==Overview==

Microtubules are hollow polymers of alphabeta-tubulin that show, GTP-dependent assembly dynamics and comprise a critical part of the, eukaryotic cytoskeleton. Initiation of new microtubules in vivo requires, gamma-tubulin, organized as an oligomer within the 2.2-MDa gamma-tubulin, ring complex (gamma-TuRC) of higher eukaryotes. Structural insight is, lacking regarding gamma-tubulin, its oligomerization and how it promotes, microtubule assembly. Here we report the 2.7-A crystal structure of human, gamma-tubulin bound to GTP-gammaS (a non-hydrolysable GTP analogue). We, observe a 'curved' conformation for gamma-tubulin-GTPgammaS, similar to, that seen for GDP-bound, unpolymerized alphabeta-tubulin. Tubulins are, thought to represent a distinct class of GTP-binding proteins, and, conformational switching in gamma-tubulin might differ from the, nucleotide-dependent switching of signalling GTPases. A crystal packing, interaction replicates the lateral contacts between alpha- and, beta-tubulins in the microtubule, and this association probably forms the, basis for gamma-tubulin oligomerization within the gamma-TuRC. Laterally, associated gamma-tubulins in the gamma-TuRC might promote microtubule, nucleation by providing a template that enhances the intrinsically weak, lateral interaction between alphabeta-tubulin heterodimers. Because they, are dimeric, alphabeta-tubulins cannot form microtubule-like lateral, associations in the curved conformation. The lateral array of, gamma-tubulins we observe in the crystal reveals a unique functional, property of a monomeric tubulin.

Microtubules are hollow polymers of alphabeta-tubulin that show GTP-dependent assembly dynamics and comprise a critical part of the eukaryotic cytoskeleton. Initiation of new microtubules in vivo requires gamma-tubulin, organized as an oligomer within the 2.2-MDa gamma-tubulin ring complex (gamma-TuRC) of higher eukaryotes. Structural insight is lacking regarding gamma-tubulin, its oligomerization and how it promotes microtubule assembly. Here we report the 2.7-A crystal structure of human gamma-tubulin bound to GTP-gammaS (a non-hydrolysable GTP analogue). We observe a 'curved' conformation for gamma-tubulin-GTPgammaS, similar to that seen for GDP-bound, unpolymerized alphabeta-tubulin. Tubulins are thought to represent a distinct class of GTP-binding proteins, and conformational switching in gamma-tubulin might differ from the nucleotide-dependent switching of signalling GTPases. A crystal packing interaction replicates the lateral contacts between alpha- and beta-tubulins in the microtubule, and this association probably forms the basis for gamma-tubulin oligomerization within the gamma-TuRC. Laterally associated gamma-tubulins in the gamma-TuRC might promote microtubule nucleation by providing a template that enhances the intrinsically weak lateral interaction between alphabeta-tubulin heterodimers. Because they are dimeric, alphabeta-tubulins cannot form microtubule-like lateral associations in the curved conformation. The lateral array of gamma-tubulins we observe in the crystal reveals a unique functional property of a monomeric tubulin.

==About this Structure==

1Z5W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1Z5W OCA].

1Z5W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GTP:'>GTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z5W OCA].

==Reference==

Line 14:

Line 13:

[[Category: Homo sapiens]]

[[Category: Single protein]]

[[Category: Agard, D.A.]]

[[Category: Agard, D A.]]

[[Category: Aldaz, H.A.]]

[[Category: Aldaz, H A.]]

[[Category: Rice, L.M.]]

[[Category: Rice, L M.]]

[[Category: Stearns, T.]]

[[Category: GTP]]

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[[Category: complex with gtp]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov~~ 12 ~~20:29~~:~~43 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:22 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1z5w.gif|left|200px]]<br />
+[[Image:1z5w.gif|left|200px]]<br /><applet load="1z5w" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1z5w" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1z5w, resolution 3.00&Aring;" />
 '''Crystal Structure of gamma-tubulin bound to GTP'''<br />
 ==Overview==
-Microtubules are hollow polymers of alphabeta-tubulin that show, GTP-dependent assembly dynamics and comprise a critical part of the, eukaryotic cytoskeleton. Initiation of new microtubules in vivo requires, gamma-tubulin, organized as an oligomer within the 2.2-MDa gamma-tubulin, ring complex (gamma-TuRC) of higher eukaryotes. Structural insight is, lacking regarding gamma-tubulin, its oligomerization and how it promotes, microtubule assembly. Here we report the 2.7-A crystal structure of human, gamma-tubulin bound to GTP-gammaS (a non-hydrolysable GTP analogue). We, observe a 'curved' conformation for gamma-tubulin-GTPgammaS, similar to, that seen for GDP-bound, unpolymerized alphabeta-tubulin. Tubulins are, thought to represent a distinct class of GTP-binding proteins, and, conformational switching in gamma-tubulin might differ from the, nucleotide-dependent switching of signalling GTPases. A crystal packing, interaction replicates the lateral contacts between alpha- and, beta-tubulins in the microtubule, and this association probably forms the, basis for gamma-tubulin oligomerization within the gamma-TuRC. Laterally, associated gamma-tubulins in the gamma-TuRC might promote microtubule, nucleation by providing a template that enhances the intrinsically weak, lateral interaction between alphabeta-tubulin heterodimers. Because they, are dimeric, alphabeta-tubulins cannot form microtubule-like lateral, associations in the curved conformation. The lateral array of, gamma-tubulins we observe in the crystal reveals a unique functional, property of a monomeric tubulin.
+Microtubules are hollow polymers of alphabeta-tubulin that show GTP-dependent assembly dynamics and comprise a critical part of the eukaryotic cytoskeleton. Initiation of new microtubules in vivo requires gamma-tubulin, organized as an oligomer within the 2.2-MDa gamma-tubulin ring complex (gamma-TuRC) of higher eukaryotes. Structural insight is lacking regarding gamma-tubulin, its oligomerization and how it promotes microtubule assembly. Here we report the 2.7-A crystal structure of human gamma-tubulin bound to GTP-gammaS (a non-hydrolysable GTP analogue). We observe a 'curved' conformation for gamma-tubulin-GTPgammaS, similar to that seen for GDP-bound, unpolymerized alphabeta-tubulin. Tubulins are thought to represent a distinct class of GTP-binding proteins, and conformational switching in gamma-tubulin might differ from the nucleotide-dependent switching of signalling GTPases. A crystal packing interaction replicates the lateral contacts between alpha- and beta-tubulins in the microtubule, and this association probably forms the basis for gamma-tubulin oligomerization within the gamma-TuRC. Laterally associated gamma-tubulins in the gamma-TuRC might promote microtubule nucleation by providing a template that enhances the intrinsically weak lateral interaction between alphabeta-tubulin heterodimers. Because they are dimeric, alphabeta-tubulins cannot form microtubule-like lateral associations in the curved conformation. The lateral array of gamma-tubulins we observe in the crystal reveals a unique functional property of a monomeric tubulin.
 ==About this Structure==
-Z5W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z5W OCA].
+Z5W is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GTP:'>GTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z5W OCA].
 ==Reference==
@@ Line 14: / Line 13: @@
 [[Category: Homo sapiens]]
 [[Category: Single protein]]
-[[Category: Agard, D.A.]]
+[[Category: Agard, D A.]]
-[[Category: Aldaz, H.A.]]
+[[Category: Aldaz, H A.]]
-[[Category: Rice, L.M.]]
+[[Category: Rice, L M.]]
 [[Category: Stearns, T.]]
 [[Category: GTP]]
@@ Line 22: / Line 21: @@
 [[Category: complex with gtp]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:29:43 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:22 2008''