1fp3
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CRYSTAL STRUCTURE OF N-ACYL-D-GLUCOSAMINE 2-EPIMERASE FROM PORCINE KIDNEY
OverviewOverview
The X-ray crystallographic structure of N-acyl-d-glucosamine 2-epimerase, (AGE) from porcine kidney, which has been identified to be a renin-binding, protein (RnBP), was determined by the multiple isomorphous replacement, method and refined at 2.0 A resolution with a final R-factor of 16.9 % for, 15 to 2.0 A resolution data. The refined structure of AGE comprised 804, amino acid residues (one dimer) and 145 water molecules. The dimer of AGE, had an asymmetric unit with approximate dimensions 46 Ax48 Ax96 A. The AGE, monomer is composed of an alpha(6)/alpha(6)-barrel, the structure of which, is found in glucoamylase and cellulase. One side of the AGE, alpha(6)/alpha(6)-barrel structure comprises long loops containing five, short beta-sheets, and contributes to the formation of a deep cleft shaped, like a funnel. The putative active-site pocket and a possible binding site, for the substrate N-acetyl-d-glucosamine (GlcNAc) were found in the cleft., The other side of the alpha(6)/alpha(6)-barrel comprises short loops and, contributes to the dimer formation. At the dimer interface, which is, composed of the short loops and alpha-helices of the subunits, five strong, ion-pair interactions were observed, which play a major role in the dimer, assembly. This completely ruled out the previously accepted hypothesis, that the formation of the RnBP homodimer and RnBP-renin heterodimer, requires the leucine zipper motif present in RnBP.
About this StructureAbout this Structure
1FP3 is a Single protein structure of sequence from Sus scrofa. Active as N-acylglucosamine 2-epimerase, with EC number 5.1.3.8 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney at 2.0 A resolution., Itoh T, Mikami B, Maru I, Ohta Y, Hashimoto W, Murata K, J Mol Biol. 2000 Nov 10;303(5):733-44. PMID:11061972
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