Tubulin_C

Tubulin/FtsZ family, C-terminal domain

• SMART accession number: SM00865
• Description: This domain is found in the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. These proteins are GTPases and are involved in polymer formation. Tubulin is the major component of microtubules, while FtsZ is the polymer-forming protein of bacterial cell division, it is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea. This is the C-terminal domain.
• Interpro abstract (IPR018316):

  This domain is found in the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. These proteins are GTPases and are involved in polymer formation. Tubulin is the major component of microtubules, while FtsZ is the polymer-forming protein of bacterial cell division, it is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea. This is the C-terminal domain.

• GO process: protein polymerization (GO:0051258), GTP catabolic process (GO:0006184)
• GO component: protein complex (GO:0043234)
• GO function: GTP binding (GO:0005525), GTPase activity (GO:0003924)

There are 5089 Tubulin_C domains in 5088 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Cellular role: replication

Literature (relevant references for this domain)

Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

• Lowe J, Amos LA
• Crystal structure of the bacterial cell-division protein FtsZ.
• Nature. 1998; 391: 203-6

Bacterial cell division ends with septation, the constriction of the cellwall and cell membranes that leads to the formation of two daughter cells.During septation, FtsZ, a protein of relative molecular mass 40,000 whichis ubiquitous in eubacteria and is also found in archaea and chloroplasts,localizes early at the division site to form a ring-shaped septum. Thisseptum is required for the mechanochemical process of membraneconstriction. FtsZ is a GTPase with weak sequence homology to tubulins.The nature of FtsZ polymers in vivo is unknown, but FtsZ can form tubules,sheets and minirings in vitro. Here we report the crystal structure at 2.8A resolution of recombinant FtsZ from the hyperthermophilic methanogenMethanococcus jannaschii. FtsZ has two domains, one of which is a GTPasedomain with a fold related to one found in the proteins p21ras andelongation factor EF-Tu. The carboxy-terminal domain, whose function isunknown, is a four-stranded beta-sheet tilted by 90 degrees against thebeta-sheet of the GTPase domain. The two domains are arranged around acentral helix. GDP binding is different from that typically found inGTPases and involves four phosphate-binding loops and a sugar-binding loopin the first domain, with guanine being recognized by residues in thecentral connecting helix. The three-dimensional structure of FtsZ issimilar to the structure of alpha- and beta-tubulin.

• Nogales E, Wolf SG, Downing KH
• Structure of the alpha beta tubulin dimer by electron crystallography.
• Nature. 1998; 391: 199-203

The alphabeta tubulin heterodimer is the structural subunit ofmicrotubules, which are cytoskeletal elements that are essential forintracellular transport and cell division in all eukaryotes. Each tubulinmonomer binds a guanine nucleotide, which is nonexchangeable when it isbound in the alpha subunit, or N site, and exchangeable when bound in thebeta subunit, or E site. The alpha- and beta-tubulins share 40% amino-acidsequence identity, both exist in several isotype forms, and both undergo avariety of posttranslational modifications. Limited sequence homology hasbeen found with the proteins FtsZ and Misato, which are involved in celldivision in bacteria and Drosophila, respectively. Here we present anatomic model of the alphabeta tubulin dimer fitted to a 3.7-A density mapobtained by electron crystallography of zinc-induced tubulin sheets. Thestructures of alpha- and beta-tubulin are basically identical: eachmonomer is formed by a core of two beta-sheets surrounded byalpha-helices. The monomer structure is very compact, but can be dividedinto three functional domains: the amino-terminal domain containing thenucleotide-binding region, an intermediate domain containing theTaxol-binding site, and the carboxy-terminal domain, which probablyconstitutes the binding surface for motor proteins.

Structure (3D structures containing this domain)

3D Structures of Tubulin_C domains in PDB

PDB code	Title
1ffx	Tubulin:stathmin-like domain complex
1fsz	Crystal structure of the cell-division protein ftsz at 2.8a resolution
1ia0	Kif1a head-microtubule complex structure in atp-form
1jff	Refined structure of alpha-beta tubulin from zinc-induced sheets stabilized with taxol
1ofu	Crystal structure of sula:ftsz from pseudomonas aeruginosa
1rlu	Mycobacterium tuberculosis ftsz in complex with gtp-gamma-s
1rq2	Mycobacterium tuberculosis ftsz in complex with citrate
1rq7	Mycobacterium tuberculosis ftsz in complex with gdp
1sa0	Tubulin-colchicine: stathmin-like domain complex
1sa1	Tubulin-podophyllotoxin: stathmin-like domain complex
1tub	Tubulin alpha-beta dimer, electron diffraction
1tvk	The binding mode of epothilone a on a,b-tubulin by electron crystallography
1w58	Ftsz gmpcpp soak i213 (m. jannaschii)
1w59	Ftsz dimer, empty (m. jannaschii)
1w5a	Ftsz dimer, mggtp soak (m. jannaschii)
1w5b	Ftsz dimer, gtp soak (m. jannaschii)
1w5e	Ftsz w319y mutant, p1 (m. jannaschii)
1w5f	Ftsz, t7 mutated, domain swapped (t. maritima)
1z2b	Tubulin-colchicine-vinblastine: stathmin-like domain complex
1z5v	Crystal structure of human gamma-tubulin bound to gtpgammas
1z5w	Crystal structure of gamma-tubulin bound to gtp
2btq	Structure of btubab heterodimer from prosthecobacter dejongeii
2hxf	Kif1a head-microtubule complex structure in amppnp-form
2hxh	Kif1a head-microtubule complex structure in adp-form
2p4n	Human monomeric kinesin (1bg2) and bovine tubulin (1jff) docked into the 9-angstrom cryo-em map of nucleotide-free kinesin complexed to the microtubule
2q1x	Crystal structure of cell division protein ftsz from mycobacterium tuberculosis in complex with citrate.
2q1y	Crystal structure of cell division protein ftsz from mycobacterium tuberculosis in complex with gtp-gamma-s
2r6r	Aquifex aeolicus ftsz
2r75	Aquifex aeolicus ftsz with 8-morpholino-gtp
2rhh	Synthetic gene encoded bacillus subtilis ftsz with bound sulfate ion
2rhj	Synthetic gene encoded bacillus subtilis ftsz with two sulfate ions and sodium ion in the nucleotide pocket
2rhl	Synthetic gene encoded bacillus subtilis ftsz ncs dimer with bound gdp
2rho	Synthetic gene encoded bacillus subtilis ftsz ncs dimer with bound gdp and gtp-gamma-s
2vam	Ftsz b. subtilis
2vap	Ftsz gdp m. jannaschii
2vaw	Ftsz pseudomonas aeruginosa gdp
2vxy	The structure of ftsz from bacillus subtilis at 1.7a resolution
2wbe	Kinesin-5-tubulin complex with amppnp
3cb2	Crystal structure of human gamma-tubulin bound to gdp
3dco	Drosophila nod (3dc4) and bovine tubulin (1jff) docked into the 11-angstrom cryo-em map of nucleotide-free nod complexed to the microtubule
3du7	Tubulin-colchicine-phomopsin a: stathmin-like domain complex
3e22	Tubulin-colchicine-soblidotin: stathmin-like domain complex
3edl	Kinesin13-microtubule ring complex
3hkb	Tubulin: rb3 stathmin-like domain complex
3hkc	Tubulin-abt751: rb3 stathmin-like domain complex
3hkd	Tubulin-tn16 : rb3 stathmin-like domain complex
3hke	Tubulin-t138067: rb3 stathmin-like domain complex

Links (links to other resources describing this domain)

• PFAM: Tubulin_C
• INTERPRO: IPR018316