3NDP

Crystal structure of human AK4(L171P)

Summary for 3NDP

• Entry DOI: 10.2210/pdb3ndp/pdb
• Descriptor: Adenylate kinase isoenzyme 4, SULFATE ION (3 entities in total)
• Functional Keywords: parallel beta-sheet, alpha-helices, transferase
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion matrix : P27144
• Total number of polymer chains: 2
• Total formula weight: 53486.78

Authors

Liu, R.,Wang, Y.,Wei, Z.,Gong, W. (deposition date: 2010-06-07, release date: 2010-06-23, Last modification date: 2024-04-03)

Primary citation

Liu, R.,Xu, H.,Wei, Z.,Wang, Y.,Lin, Y.,Gong, W.
Crystal structure of human adenylate kinase 4 (L171P) suggests the role of hinge region in protein domain motion
Biochem.Biophys.Res.Commun., 379:92-97, 2009

PubMed 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.

PubMed: 19073142
DOI: 10.1016/j.bbrc.2008.12.012

Experimental method

X-RAY DIFFRACTION (2.3 Å)