Tubulin: Difference between revisions
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Tubulin is a [[globular protein|globular protein]] of which there are two forms; alpha and beta. These "homologous 50 kDa subunits. . . assemble in a helical array of alternating tubulin types" to form [[Microtubules|microtubules]]. Electron crystallography was used to analyse the 3-D strucutre of tubulin, it was found that "tubulins are members of the [[P-loop NTPase family|P-loop NTPase family]] and contain a [[nucelotide-binding site|nucelotide-binding site]] adjacent to the P-loop". It was also deteremined that alpha and beta types show high levels of similarity. It is thought that tubulin only exists in eukaryotes, although a [[prokaryote|prokaryote]] homolog has been identified, protein FtsZ. "This protein particitpates in [[bacterial cell division|bacterial cell division]], forming ring structures. These observations suggest that tubulins may have been evolved from ancient cell-division protein." <ref>Berg, Tymoczko and Stryer.(2006). Biochemistry. sixth edition. (page 989-990)</ref><ref>Berg, tymoczko and Stryer. (2006). Biochemistry. sixth edition.</ref> | |||
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Revision as of 16:44, 23 October 2012
Tubulin is a globular protein of which there are two forms; alpha and beta. These "homologous 50 kDa subunits. . . assemble in a helical array of alternating tubulin types" to form microtubules. Electron crystallography was used to analyse the 3-D strucutre of tubulin, it was found that "tubulins are members of the P-loop NTPase family and contain a nucelotide-binding site adjacent to the P-loop". It was also deteremined that alpha and beta types show high levels of similarity. It is thought that tubulin only exists in eukaryotes, although a prokaryote homolog has been identified, protein FtsZ. "This protein particitpates in bacterial cell division, forming ring structures. These observations suggest that tubulins may have been evolved from ancient cell-division protein." [1][2]