Structural highlights
Function
[KAD4_HUMAN] Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. May also be active with GTP (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of human adenylate kinase 4 (L171P) suggests the role of hinge region in protein domain motion.,Liu R, Xu H, Wei Z, Wang Y, Lin Y, Gong W Biochem Biophys Res Commun. 2009 Jan 30;379(1):92-7. Epub 2008 Dec 13. PMID:19073142[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2009 Jan 30;379(1):92-7. Epub 2008 Dec 13. PMID:19073142 doi:10.1016/j.bbrc.2008.12.012
