title: Crystal structure of human adenylate kinase 4 (L171P) suggests the role of hinge region in protein domain motion.
abstract: It is well known that motion of LID and NMP-binding (NMP(bind)) domains in adenylate kinase (AK) is important in ligand binding and catalysis. However, the nature of such domain motions is poorly characterized. One of the critical hinge regions is hinge IV, which connects the CORE and LID domains. In addition, the hinge IV contains a strictly conserved residue, L171, in the AK family. To investigate the role of hinge IV, crystal structure of human adenylate kinase 4 (AK4) L171P mutant was determined. This mutation dramatically changes the orientation of the LID domain, which could be described as a novel twisted-and-closed conformation in contrast to the open and closed conformations in other AKs. This mutant provides a new example of domain motions in AK family.
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, People's Republic of China.
authors.forename: Rujuan
authors.initials: R
authors.lastname: Liu
authors.forename: Hang
authors.initials: H
authors.lastname: Xu
authors.forename: Zhiyi
authors.initials: Z
authors.lastname: Wei
authors.forename: Yanli
authors.initials: Y
authors.lastname: Wang
authors.forename: Yajing
authors.initials: Y
authors.lastname: Lin
authors.forename: Weimin
authors.initials: W
authors.lastname: Gong
mesh_terms: D000263:Adenylate Kinase / Q000737:chemistry* / Q000235:genetics; D018360:Crystallography, X-Ray; D006801:Humans; D007930:Leucine / Q000737:chemistry / Q000235:genetics; D009154:Mutation; D011392:Proline / Q000737:chemistry / Q000235:genetics; D017434:Protein Structure, Tertiary
chemical_list: D011392:Proline; D000263:Adenylate Kinase; D007930:Leucine