プロトマー
- 関
- protein subunit
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/12/18 20:51:27」(JST)
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In structural biology, a protomer is the structural unit of an oligomeric protein. It is the smallest unit composed of at least two different protein chains that form a larger heterooligomer by association of two or more copies of this unit.
The term was introduced by Chetverin [1] to make nomenclature in Na/K-ATPase unambiguous. Na/K-consists of an α- and a β-subunit (plus a proteolipid, called γ-subunit). At the time it was unclear how many of each work together. In addition, when people spoke of a dimer, did they refer to αβ or to (αβ)2? Chetverin suggested to call αβ a protomer and (αβ)2 a diprotomer.
Protomers usually arrange in cyclic symmetry to form closed point group symmetries.
Examples
Hemoglobin is a heterotetramer consisting of four subunits (two α and two β). However, structurally and functionally hemoglobin is described better as (αβ)2, we say it is a dimer of two αβ-protomers, that is, a diprotomer.[2]
Aspartate carbamoyltransferase has a α6β6 subunit composition. The six αβ-protomers are arranged in D3 symmetry.
Viral capsid often are made from protomers.
References
- ^ Chetverin, A.B. (1986). "Evidence for a diprotomeric structure of Na, K-ATPase: Accurate determination of protein concentration and quantitative end-group analysis". FEBS Lett. 196: 121–125. doi:10.1016/0014-5793(86)80225-3. PMID 3002859.
- ^ Buxbaum, E. (2007). Fundamentals of protein structure and function. New York: Springer. pp. 105–120. ISBN 978-0-387-26352-6.
External links
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Japanese Journal
- 野田 展生
- 日本結晶学会誌 54(3), 166-171, 2012-06-30
- … Atg7 protomer is comprised of two globular domains, the N-terminal domain (NTD) and the C-terminal domain (CTD), and forms a homodimer through CTD. … Atg8 is then transferred to Atg3 bound to the NTD of the opposite protomer within an Atg7 dimer via a trans mechanism. …
- NAID 10030793233
- Crystal structure of the octameric pore of staphylococcal γ-hemolysin reveals the β-barrel pore formation mechanism by two components
- Proceedings of the National Academy of Sciences of the United States of America 108(42), 17314-17319, 2011-10-18
- … elaborate molecular machinery involved in pore formation by two different molecules, in which inter-protomer electrostatic interactions using loops connecting β2 and β3 (loop A:Asp43-Lys48 of LukF and Lys37-Lys43 of Hlg2) play pivotal roles as the structural determinants for assembly through unwinding of the N-terminal β-strands (amino-latch) of the adjacent protomer, releasing the transmembrane stem domain folded into a β-sheet in the monomer (pre-stem), and interaction with the adjacent protomer. …
- NAID 80022107886
- Structures of the SEp22 dodecamer, a Dps-like protein from Salmonella enterica subsp. enterica serovar Enteritidis
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- Structural Biology and Crystallization Communications : Acta Crystallographica Section F 67(1), 17-22, 2011-01
- … The SEp22 protomers form a dodecameric shell with 23 symmetry and a single iron ion per protomer was found at the ferroxidase centre in the iron-soaked form. …
- NAID 120002696074
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- The replaced amino acids were located in a refined 3-dimensional computer model of the HAV protomer (11), and their relative distances to residues 1102, 1171 and 1176, constituents of the immunodominant site (12), and to residue ...
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