01831naa a2200253 a 450000100080000000500110000800800410001902400280006010000140008824501360010226000090023852010390024765000260128665000120131265000290132465300250135365300390137865300310141765300340144870000140148270000170149670000190151377300450153210096102020-01-15       2008    bl uuuu     u00u1 u    #d7 a10.1002/prot.219562DOI1 aKUSER, P.  aCrystal structure of yeast hexokinase PI in complex with glucoseba classical "induced fit" example revised.h[electronic resource]  c2008  aHexokinase is the first enzyme in the glycolytic pathway that catalyzes the transfer of a phosphoryl group from ATP to glucose to form glucose-6-phosphate and ADP. Two yeast hexokinase isozymes are known, namely PI and PII. Here we redetermined the crystal structure of yeast hexokinase PI from Saccharomyces cerevisiae as a complex with its substrate, glucose, and refined it at 2.95 A resolution. Comparison of the holo-PI yeast hexokinase and apo-hexokinase structures shows in detail the rigid body domain closure and specific loop movements as glucose binds and sheds more light on structural basis of the "induced fit" mechanism of reaction in the HK enzymatic action. We also performed statistical coupling analysis of the hexokinase family, which reveals two co-evolved continuous clusters of amino acid residues and shows that the evolutionary coupled amino acid residues are mostly confined to the active site and the hinge region, further supporting the importance of these parts of the protein for the enzymatic catalysis.  aAnálise estatística  aGlicose  aSaccharomyces Cerevisiae  aEstrutura cristalina  aEstrutura de raio-X de hexoquinase  aHexokinase X-ray structure  aStatistical coupling analysis1 aCUPRI, F.1 aBLEICHER, L.1 aPOLIKARPOV, I.  tProteinsgv. 72, n. 2, p. 731-740, 2008.