1h6c: Difference between revisions
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OXIDIZED PRECURSOR FORM OF GLUCOSE-FRUCTOSE OXIDOREDUCTASE FROM ZYMOMONAS MOBILIS COMPLEXED WITH SUCCINATE
OverviewOverview
The NADP(H)-dependent enzyme glucose-fructose oxidoreductase (GFOR) is a, classic example of a redox protein that is translocated across a membrane, in fully folded form. GFOR is synthesized in the cytoplasm with a, 52-residue signal peptide, giving a precursor form, preGFOR, that is fully, active and has its cofactor tightly bound. A twin-arginine motif in the, signal peptide directs it to a Sec-independent pathway by which it is, translocated, in fully folded form, into the periplasm where it functions, to produce sorbitol for osmoprotection. We have determined the crystal, structures of four different forms of preGFOR, (i) oxidized preGFOR, with, succinate bound in the active site, (ii) oxidized preGFOR with glycerol, bound, (iii) reduced preGFOR in 0.3 M glucose, and (iv) reduced ... [(full description)]
About this StructureAbout this Structure
1H6C is a [Single protein] structure of sequence from [Zymomonas mobilis] with NDP, SIN and GOL as [ligands]. Active as [Glucose--fructose oxidoreductase], with EC number [1.1.99.28]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands., Nurizzo D, Halbig D, Sprenger GA, Baker EN, Biochemistry. 2001 Nov 20;40(46):13857-67. PMID:11705375
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