1tub

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1tub" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tub, resolution 3.7&Aring;" /> '''TUBULIN ALPHA-BETA DI...)
Line 1: Line 1:
-
[[Image:1tub.jpg|left|200px]]<br /><applet load="1tub" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1tub.jpg|left|200px]]<br /><applet load="1tub" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1tub, resolution 3.7&Aring;" />
caption="1tub, resolution 3.7&Aring;" />
'''TUBULIN ALPHA-BETA DIMER, ELECTRON DIFFRACTION'''<br />
'''TUBULIN ALPHA-BETA DIMER, ELECTRON DIFFRACTION'''<br />
==Overview==
==Overview==
-
The alphabeta tubulin heterodimer is the structural subunit of, microtubules, which are cytoskeletal elements that are essential for, intracellular transport and cell division in all eukaryotes. Each tubulin, monomer binds a guanine nucleotide, which is nonexchangeable when it is, bound in the alpha subunit, or N site, and exchangeable when bound in the, beta subunit, or E site. The alpha- and beta-tubulins share 40% amino-acid, sequence identity, both exist in several isotype forms, and both undergo a, variety of posttranslational modifications. Limited sequence homology has, been found with the proteins FtsZ and Misato, which are involved in cell, division in bacteria and Drosophila, respectively. Here we present an, atomic model of the alphabeta tubulin dimer fitted to a 3.7-A density map, obtained by electron crystallography of zinc-induced tubulin sheets. The, structures of alpha- and beta-tubulin are basically identical: each, monomer is formed by a core of two beta-sheets surrounded by, alpha-helices. The monomer structure is very compact, but can be divided, into three functional domains: the amino-terminal domain containing the, nucleotide-binding region, an intermediate domain containing the, Taxol-binding site, and the carboxy-terminal domain, which probably, constitutes the binding surface for motor proteins.
+
The alphabeta tubulin heterodimer is the structural subunit of microtubules, which are cytoskeletal elements that are essential for intracellular transport and cell division in all eukaryotes. Each tubulin monomer binds a guanine nucleotide, which is nonexchangeable when it is bound in the alpha subunit, or N site, and exchangeable when bound in the beta subunit, or E site. The alpha- and beta-tubulins share 40% amino-acid sequence identity, both exist in several isotype forms, and both undergo a variety of posttranslational modifications. Limited sequence homology has been found with the proteins FtsZ and Misato, which are involved in cell division in bacteria and Drosophila, respectively. Here we present an atomic model of the alphabeta tubulin dimer fitted to a 3.7-A density map obtained by electron crystallography of zinc-induced tubulin sheets. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three functional domains: the amino-terminal domain containing the nucleotide-binding region, an intermediate domain containing the Taxol-binding site, and the carboxy-terminal domain, which probably constitutes the binding surface for motor proteins.
==About this Structure==
==About this Structure==
-
1TUB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with GTP, GDP and TXL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TUB OCA].
+
1TUB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=GTP:'>GTP</scene>, <scene name='pdbligand=GDP:'>GDP</scene> and <scene name='pdbligand=TXL:'>TXL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TUB OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
-
[[Category: Downing, K.H.]]
+
[[Category: Downing, K H.]]
[[Category: Nogales, E.]]
[[Category: Nogales, E.]]
[[Category: GDP]]
[[Category: GDP]]
Line 23: Line 23:
[[Category: microtubules]]
[[Category: microtubules]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:35:47 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:17:23 2008''

Revision as of 13:17, 21 February 2008


1tub, resolution 3.7Å

Drag the structure with the mouse to rotate

TUBULIN ALPHA-BETA DIMER, ELECTRON DIFFRACTION

Overview

The alphabeta tubulin heterodimer is the structural subunit of microtubules, which are cytoskeletal elements that are essential for intracellular transport and cell division in all eukaryotes. Each tubulin monomer binds a guanine nucleotide, which is nonexchangeable when it is bound in the alpha subunit, or N site, and exchangeable when bound in the beta subunit, or E site. The alpha- and beta-tubulins share 40% amino-acid sequence identity, both exist in several isotype forms, and both undergo a variety of posttranslational modifications. Limited sequence homology has been found with the proteins FtsZ and Misato, which are involved in cell division in bacteria and Drosophila, respectively. Here we present an atomic model of the alphabeta tubulin dimer fitted to a 3.7-A density map obtained by electron crystallography of zinc-induced tubulin sheets. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three functional domains: the amino-terminal domain containing the nucleotide-binding region, an intermediate domain containing the Taxol-binding site, and the carboxy-terminal domain, which probably constitutes the binding surface for motor proteins.

About this Structure

1TUB is a Protein complex structure of sequences from Sus scrofa with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the alpha beta tubulin dimer by electron crystallography., Nogales E, Wolf SG, Downing KH, Nature. 1998 Jan 8;391(6663):199-203. PMID:9428769

Page seeded by OCA on Thu Feb 21 15:17:23 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools