Identification of phosphate binding residues of Escherichia coli ATP synthase.
نویسندگان
چکیده
Four positively-charged residues, namely betaLys-155, betaArg-182, betaArg-246, and alphaArg-376 have been identified as Pi binding residues in Escherichia coli ATP synthase. They form a triangular Pi binding site in catalytic site betaE where substrate Pi initially binds for ATP synthesis in oxidative phosphorylation. Positive electrostatic charge in the vicinity of betaArg-246 is shown to be one important component of Pi binding.
منابع مشابه
Role of Charged Residues in the Catalytic Sites of Escherichia coli ATP Synthase
Here we describe the role of charged amino acids at the catalytic sites of Escherichia coli ATP synthase. There are four positively charged and four negatively charged residues in the vicinity of of E. coli ATP synthase catalytic sites. Positive charges are contributed by three arginine and one lysine, while negative charges are contributed by two aspartic acid and two glutamic acid residues. R...
متن کاملModulation of charge in the phosphate binding site of Escherichia coli ATP synthase.
This paper presents a study of the role of positive charge in the P(i) binding site of Escherichia coli ATP synthase, the enzyme responsible for ATP-driven proton extrusion and ATP synthesis by oxidative phosphorylation. Arginine residues are known to occur with high propensity in P(i) binding sites of proteins generally and in the P(i) binding site of the betaE catalytic site of ATP synthase s...
متن کاملFunctional arginyl residues as ATP binding sites of glutamine synthetase and carbamyl phosphate synthetase.
The reaction of phenylglyoxal with two enzymes in which ATP plays a complex role has been studied. Both ovine brain glutamine synthetase and Escherichia coli carbamyl phosphate synthetase [carbamoyl-phosphate synthase (glutamine); ATP:carbamate phosphotransferase (dephosphorylating, amido-transferring); EC 2.7.2.9]were inactivated by phenylglyoxal. The specificity of this reagent for arginyl re...
متن کاملMovement of the biotin carboxylase B-domain as a result of ATP binding.
Acetyl-CoA carboxylase catalyzes the first committed step in fatty acid synthesis. In Escherichia coli, the enzyme is composed of three distinct protein components: biotin carboxylase, biotin carboxyl carrier protein, and carboxyltransferase. The biotin carboxylase component has served for many years as a paradigm for mechanistic studies devoted toward understanding more complicated biotin-depe...
متن کاملRole of Asn-243 in the Phosphate-binding Subdomain of Catalytic Sites of Escherichia coli F1-ATPase*
In the catalytic mechanism of ATP synthase, phosphate (Pi) binding and release steps are believed to be correlated to -subunit rotation, and Pi binding is proposed to be prerequisite for binding ADP in the face of high cellular [ATP]/[ADP] ratios. In x-ray structures, residue Asn-243 appears centrally located in the Pibinding subdomain of catalytic sites. Here we studied the role of Asn-243 in ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید
ثبت ناماگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید
ورودعنوان ژورنال:
- Journal of bioenergetics and biomembranes
دوره 37 6 شماره
صفحات -
تاریخ انتشار 2005