English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/17892
Título

Protein flexibility and metal coordination changes in DHAP-dependent aldolases

AutorJiménez, Aurora; Clapés Saborit, Pere; Crehuet, Ramón
Palabras claveDensity functional calculations
Enzyme catalysis
Metalloproteins
Protein flexibility
Reaction mechanisms
Fecha de publicación26-ene-2009
EditorJohn Wiley & Sons
CitaciónChemistry - A European Journal 15(6): 1422-1428 (2009)
ResumenThe mobility of rhamnulose-1-phosphate aldolase (RhuA) was analysed with a normal mode description and high level calculations on models of the active site. We report the connection between the mobility and the chemical properties of the active site, and compare them to a closely related enzyme, fuculose-1-phosphate aldolase (FucA). Calculations show that the different coordination number for the zinc ion, reported in the crystal structures of RhuA and FucA, was due to a different spatial arrangement of the residues, not to their different chemical nature. Moreover, the metal coordination change is correlated with activity. The domain mobility of the enzyme can reshape the active site of RhuA into the arrangement found in the FucA structure, and vice-versa. This has a direct influence on the energy barrier for the aldol reaction catalyzed by these enzymes, thus showing a coupling of the domain movements and the catalytic effects. Hence domain movements and the coordination chemistry of the active site metal suggest an explanation of why these enzymes have similar experimental turnover rates.
Descripción7 pages, 5 figures, 2 tables.-- PMID: 19115296 [PubMed].-- Available online Dec 29, 2008.
Versión del editorhttp://dx.doi.org/10.1002/chem.200801223
URIhttp://hdl.handle.net/10261/17892
DOI10.1002/chem.200801223
ISSN0947-6539
Aparece en las colecciones: (IQAC) Artículos
Ficheros en este ítem:
No hay ficheros asociados a este ítem.
Mostrar el registro completo
 

Artículos relacionados:


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.