1tub: Difference between revisions

Revision as of 17:22, 27 July 2008

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File:1tub.png

Template:STRUCTURE 1tub

TUBULIN ALPHA-BETA DIMER, ELECTRON DIFFRACTIONTUBULIN ALPHA-BETA DIMER, ELECTRON DIFFRACTION

Template:ABSTRACT PUBMED 9428769

About this StructureAbout this Structure

1TUB is a Protein complex structure of sequences from Sus scrofa. Full crystallographic information is available from OCA.

ReferenceReference

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 Sun Jul 27 17:22:41 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1tub.jpg|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1tub|  PDB=1tub  |  SCENE=  }}
-'''TUBULIN ALPHA-BETA DIMER, ELECTRON DIFFRACTION'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_9428769}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9428769 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9428769}}
 ==About this Structure==
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 [[Category: Gtpase]]
 [[Category: Microtubule]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 10:22:29 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:22:41 2008''