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Titolo:
Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation
Autore:
Aleshin, AE; Kirby, C; Liu, XF; Bourenkov, GP; Bartunik, HD; Fromm, HJ; Honzatko, RB;
Indirizzi:
Iowa State Univ, Dept Biochem Biophys & Mol Biol, Ames, IA 50011 USA Iowa State Univ Ames IA USA 50011 Biophys & Mol Biol, Ames, IA 50011 USA DESY, Max Planck Res Unit Struct Mol Biol, MPG, ASMB, D-22603 Hamburg, Germany DESY Hamburg Germany D-22603 l Biol, MPG, ASMB, D-22603 Hamburg, Germany
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 4, volume: 296, anno: 2000,
pagine: 1001 - 1015
SICI:
0022-2836(20000303)296:4<1001:CSOMMH>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT-BRAIN HEXOKINASE; PERMEABILITY TRANSITION PORE; ACTIVE-SITE; OXIDATIVE-PHOSPHORYLATION; ADENYLATE TRANSLOCATOR; MITOCHONDRIAL PORIN; PROTEIN MODELS; TERMINAL HALF; N-TERMINUS; GLUCOSE;
Keywords:
hexokinase I; brain hexokinase; X-ray structure; glycolysis; allosteric enzyme;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Honzatko, RB Iowa State Univ, Dept Biochem Biophys & Mol Biol, Ames, IA 50011 USA Iowa State Univ Ames IA USA 50011 l Biol, Ames, IA 50011 USA
Citazione:
A.E. Aleshin et al., "Crystal structures of mutant monomeric hexokinase I reveal multiple ADP binding sites and conformational changes relevant to allosteric regulation", J MOL BIOL, 296(4), 2000, pp. 1001-1015

Abstract

Hexokinase I, the pacemaker of glycolysis in brain tissue, is composed of two structurally similar halves connected by an alpha-helix. The enzyme dimerizes at elevated protein concentrations in solution and in crystal structures; however, almost all published data reflect the properties of a hexokinase I monomer in solution. Crystal structures of mutant forms of recombinant human hexokinase I, presented here, reveal the enzyme monomer for the first time. The mutant hexokinases bind both glucose 6-phosphate and glucose with high affinity to their N and C-terminal halves, and ADP, also with high affinity, to a site near the N terminus of the polypeptide chain. Exposure of the monomer crystals to ADP in the complete absence of glucose 6-phosphate reveals a second binding site for adenine nucleotides at the putative active site (C-half), with conformational changes extending 15 Angstrom to the contact interface between the N and C-halves. The structures reveal distinct conformational states for the C-half and a rigid-body rotation of theN-half, as possible elements of a structure-based mechanism for allostericregulation of catalysis. (C) 2000 Academic Press.

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Documento generato il 19/09/20 alle ore 12:47:29