caa a22 4500 606209441 CHVBK 20210128101028.0 cr unu---uuuuu 210128e20150501xx s 000 0 eng 10.1007/s00425-014-2236-6 doi (NATIONALLICENCE)springer-10.1007/s00425-014-2236-6 Crystal structure of a plant albumin from Cicer arietinum (chickpea) possessing hemopexin fold and hemagglutination activity [Elektronische Daten] [Urvashi Sharma, Uma Katre, C. Suresh] Main conclusion : Crystal structure of a reported PA2 albumin from Cicer arietinum shows that it belongs to hemopexin fold family, has four beta-propeller motifs and possesses hemagglutination activity, making it different from known legume lectins. A plant albumin (PA2) from Cicer arietinum, presumably a lectin (CAL) owing to its hemagglutination activity which is inhibited by complex sugars as well as glycoproteins such as fetuin, desialylated fetuin and fibrinogen. The three-dimensional structure of this homodimeric protein has been determined using X-ray crystallography at 2.2 Å in two crystal forms: orthorhombic (P21212) and trigonal (P3). The structure determined using molecular replacement method and refined in orthorhombic crystal form reached R-factors R free 22.6% and R work 18.2% and in trigonal form had 22.3 and 17.9% in the resolution range of 20.0-2.2 and 35.3-2.2 Å, respectively. Interestingly, unlike the known legume lectin fold, the structure of this homodimeric hemagglutinin belonged to hemopexin fold that consisted of four-bladed β-propeller architecture. Each subunit has a central cavity forming a channel, inside of which is lined with hydrophobic residues. The channel also bears binding sites for ligands such as calcium, sodium and chloride ions, iodine atom in the case of iodine derivative and water molecules. However, none of these ligands seem important for the sugar recognition. No monosaccharide sugar specificity could be detected using hemagglutination inhibition. Chemical modification studies identified a potential sugar-binding site per subunit molecule. Comparison of C-alpha atom positions in subunit structures showed that the deviations between the two crystal forms were more with respect to blades I and IV. Differences also existed between subunits in two forms in terms of type and site of ligand binding. Springer-Verlag Berlin Heidelberg, 2015 Chickpea lectin nationallicence PA2 albumin nationallicence Beta-propeller fold nationallicence Sugar binding nationallicence Complex sugars nationallicence Chemical modification nationallicence CAL : Cicer arietinum lectin nationallicence DEPC : Diethyl pyrocarbonate nationallicence WRK : Woodward's reagent K nationallicence PMSF : Phenylmethylsulfonyl fluoride nationallicence TNBS : Trinitrobenzenesulphonic acid nationallicence NBS : N-bromosuccinimide nationallicence PG : Phenylglyoxal nationallicence Sharma Urvashi Division of Biochemical Sciences, CSIR-National Chemical Laboratory, 411008, Pune, India aut Katre Uma Division of Biochemical Sciences, CSIR-National Chemical Laboratory, 411008, Pune, India aut Suresh C. Division of Biochemical Sciences, CSIR-National Chemical Laboratory, 411008, Pune, India aut Planta Springer Berlin Heidelberg 241/5(2015-05-01), 1061-1073 0032-0935 241:5<1061 2015 241 425 https://doi.org/10.1007/s00425-014-2236-6 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00425-014-2236-6 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Sharma Urvashi Division of Biochemical Sciences, CSIR-National Chemical Laboratory, 411008, Pune, India aut NATIONALLICENCE 700 1- Katre Uma Division of Biochemical Sciences, CSIR-National Chemical Laboratory, 411008, Pune, India aut NATIONALLICENCE 700 1- Suresh C. Division of Biochemical Sciences, CSIR-National Chemical Laboratory, 411008, Pune, India aut NATIONALLICENCE 773 0- Planta Springer Berlin Heidelberg 241/5(2015-05-01), 1061-1073 0032-0935 241:5<1061 2015 241 425