Literature summary for 2.7.4.2 extracted from

Olson, A.L.; Yao, H.; Herdendorf, T.J.; Miziorko, H.M.; Hannongbua, S.; Saparpakorn, P.; Cai, S.; Sem, D.S.
Substrate induced structural and dynamics changes in human phosphomevalonate kinase and implications for mechanism (2008), Proteins, 75, 127-138.

Crystallization (Commentary)

Crystallization (Comment)	Organism
NMR-based dynamics and chemical shift experiments of enzyme in complex with MgADP, mevalonate 5-phosphate and the ternary complex. Binding of mevalonate 5-phosphate causes the protein to compress, whereas subsequent binding of MgADP opens the structure. Mevalonate 5-phosphate causes movement around a hinge region to permit domain closure. Amino acids H55 and R93 may act as hinge residues, D163 may be a hinge residue for the lid region. Binding of ATP or ADP causes similar conformational changes. The first nine residues of the N-terminus are highly disordered	Homo sapiens

Crystallization (Comment)

Organism

NMR-based dynamics and chemical shift experiments of enzyme in complex with MgADP, mevalonate 5-phosphate and the ternary complex. Binding of mevalonate 5-phosphate causes the protein to compress, whereas subsequent binding of MgADP opens the structure. Mevalonate 5-phosphate causes movement around a hinge region to permit domain closure. Amino acids H55 and R93 may act as hinge residues, D163 may be a hinge residue for the lid region. Binding of ATP or ADP causes similar conformational changes. The first nine residues of the N-terminus are highly disordered

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

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Release 2023.1 (January 2023)