3bif
From Proteopedia
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6-PHOSPHOFRUCTO-2-KINASE/FRUCTOSE-2,6-BISPHOSPHATASE EMPTY 6-PF-2K ACTIVE SITE
Overview
The bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatase plays an essential role in the regulation of glucose, metabolism by both producing and degrading Fru-2,6-P(2) via its distinct, catalytic activities. The 6-PF-2-K and Fru-2,6-P(2)ase active sites are, located in separate domains of the enzyme. The kinase domain is, structurally related to the superfamily of mononucleotide binding proteins, that includes adenylate kinase and the G-proteins. We have determined, three new structures of the enzymatic monomer, each with a different, ligand in the ATP binding site of the 6-PF-2-K domain (AMP-PNP, PO(4), and, water). A comparison of these three new structures with the, ATPgammaS-bound 6-PF-2-K domain reveals a rearrangement of a helix that is, dependent on the ligand ... [(full description)]
About this Structure
3BIF is a [Single protein] structure of sequence from [Rattus norvegicus] with BOG, PO4 and SIN as [ligands]. Active as [6-phosphofructo-2-kinase], with EC number [2.7.1.105]. Structure known Active Sites: S1, S2 and S3. Full crystallographic information is available from [OCA].
Reference
A switch in the kinase domain of rat testis 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase., Yuen MH, Wang XL, Mizuguchi H, Uyeda K, Hasemann CA, Biochemistry. 1999 Sep 21;38(38):12333-42. PMID:10493801
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