Re: [ccp4bb] NADP binding protein without Rossmann fold.
Dear all, Thank you very much for your cooperation. Regards, Sudipta. Sudipta Bhattacharyya. Senior Research Fellow, Department of Biotechnology, Indian Institute of Technology Kharagpur, India.
[ccp4bb] NADP binding protein without Rossmann fold.
Dear all, I have biochemically characterized one enzyme that can dephosphorylate NADP+ / NADPH. Recently, I have also solved the crystal structure of the protein with bound NADP+. The important thing is that, the protein do not have the Rossmann fold or the dinucleotide binding fold. Can any one please cite or suggest any other example of such type of anomaly? Is there any example of non-classical Rossmann fold bearing proteins? Thanks, Sudipta. Sudipta Bhattacharyya. Senior Research Fellow, Department of Biotechnology, Indian Institute of Technology Kharagpur, India.
Re: [ccp4bb] NADP binding protein without Rossmann fold.
Zitat von Sudipta Bhattacharyya sudiptabhattacharyya.iit...@gmail.com: Dear all, I have biochemically characterized one enzyme that can dephosphorylate NADP+ / NADPH. Recently, I have also solved the crystal structure of the protein with bound NADP+. The important thing is that, the protein do not have the Rossmann fold or the dinucleotide binding fold. Can any one please cite or suggest any other example of such type of anomaly? Is there any example of non-classical Rossmann fold bearing proteins? Thanks, Sudipta. Dear Sudipta, AKR enzymes (aldo/keto reductases; see www.med.upenn.edu/akr/ and www.ncbi.nlm.nih.gov/pubmed/20887732) bind NAD(P) and have an (alpha/beta)8 barrel motif. Best wishes, Karsten Niefind - Karsten Niefind, PhD University of Cologne Department of Chemistry Otto-Fischer-Str. 12-14 D-50674 Cologne Tel.: +49 (0)221 4706444 Fax: +49 (0)221 4703244
Re: [ccp4bb] NADP binding protein without Rossmann fold.
Many flavin reductases and monooxygenases bind NAD(P)H without the Rossmann fold. See the review by Massey (2000) The chemical and biological versatility of riboflavin. Biochem. Soc. Trans. 28(4):283-296. Also, ALDHs bind NAD(P)+ with a Rossmann-like fold, which is considered to be a nonclassical Rossmann fold. See Liu, et al., Nat. Struct. Biol. 1997. On Aug 12, 2012, at 3:20 PM, Karsten Niefind wrote: Zitat von Sudipta Bhattacharyya sudiptabhattacharyya.iit...@gmail.com: Dear all, I have biochemically characterized one enzyme that can dephosphorylate NADP+ / NADPH. Recently, I have also solved the crystal structure of the protein with bound NADP+. The important thing is that, the protein do not have the Rossmann fold or the dinucleotide binding fold. Can any one please cite or suggest any other example of such type of anomaly? Is there any example of non-classical Rossmann fold bearing proteins? Thanks, Sudipta. Dear Sudipta, AKR enzymes (aldo/keto reductases; see www.med.upenn.edu/akr/ and www.ncbi.nlm.nih.gov/pubmed/20887732) bind NAD(P) and have an (alpha/beta)8 barrel motif. Best wishes, Karsten Niefind - Karsten Niefind, PhD University of Cologne Department of Chemistry Otto-Fischer-Str. 12-14 D-50674 Cologne Tel.: +49 (0)221 4706444 Fax: +49 (0)221 4703244
Re: [ccp4bb] NADP binding protein without Rossmann fold.
Hello, You could look at this family of enzymes, http://scop.mrc-lmb.cam.ac.uk/scop/data/scop.b.d.jc.b.b.html [the sulfolactate dehydrogenase-like family] No Rossman fold there. HTH, Fred. Dear all, I have biochemically characterized one enzyme that can dephosphorylate NADP+ / NADPH. Recently, I have also solved the crystal structure of the protein with bound NADP+. The important thing is that, the protein do not have the Rossmann fold or the dinucleotide binding fold. Can any one please cite or suggest any other example of such type of anomaly? Is there any example of non-classical Rossmann fold bearing proteins? Thanks, Sudipta. Sudipta Bhattacharyya. Senior Research Fellow, Department of Biotechnology, Indian Institute of Technology Kharagpur, India. -- F.M.D. Vellieux (B.Sc., Ph.D., hdr) IBS / ELMA 41 rue Jules Horowitz 38027 Grenoble Cedex 01 France Tel: +33 438789605 Fax: +33 438785494
