Structures of pyruvate kinases display evolutionarily divergent allosteric strategies

dc.contributor.author	Morgan, Hugh P.	en_US
dc.contributor.author	Zhong, Wenhe	en_US
dc.contributor.author	McNae, Iain W.	en_US
dc.date.accessioned	2016-07-18T06:49:05Z
dc.date.available	2016-07-18T06:49:05Z
dc.date.issued	2014	en_US
dc.identifier.other	HPU4160413	en_US
dc.identifier.uri	https://lib.hpu.edu.vn/handle/123456789/22254	en_US
dc.description.abstract	The transition between the inactive T-state (apoenzyme) and active R-state (effector bound enzyme) of Trypanosoma cruzi pyruvate kinase (PYK) is accompanied by a symmetrical 8 rigid body rocking motion of the A- and C-domain cores in each of the four subunits, coupled with the formation of additional salt bridges across two of the four subunit interfaces.	en_US
dc.format.extent	14 p.	en_US
dc.format.mimetype	application/pdf	en_US
dc.language.iso	en	en_US
dc.subject	Biochemistry	en_US
dc.subject	Biophysics	en_US
dc.subject	Structural biology	en_US
dc.subject	Apoenzyme	en_US
dc.subject	Leishmania	en_US
dc.subject	Trypanosoma	en_US
dc.title	Structures of pyruvate kinases display evolutionarily divergent allosteric strategies	en_US
dc.type	Article	en_US
dc.size	2.13MB	en_US
dc.department	Education	en_US