5f24 | pdb_00005f24

Crystal structure of dual specific IMPase/NADP phosphatase bound with D-inositol-1-phosphate

spinqualitylabelsall models 5f24, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5f24 is a 2 chain structure with sequence from "micrococcus_aureus"_(rosenbach_1884)_zopf_1885 "micrococcus aureus" (rosenbach 1884) zopf 1885. This structure supersedes the now removed PDB entry 4g60. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CL, GOL, IPD, P6G, PG4 Activity: Inositol-phosphate phosphatase, with EC number 3.1.3.25 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed NADP(H)/NAD(H) homeostasis has long been identified to play a pivotal role in the mitigation of reactive oxygen stress (ROS) in the intracellular milieu and is therefore critical for the progression and pathogenesis of many diseases. NAD(H) kinases and NADP(H) phosphatases are two key players in this pathway. Despite structural evidence demonstrating the existence and mode of action of NAD(H) kinases, the specific annotation and the mode of action of NADP(H) phosphatases remains obscure. Here, structural evidence supporting the alternative role of inositol monophosphatase (IMPase) as an NADP(H) phosphatase is reported. Crystal structures of staphylococcal dual-specific IMPase/NADP(H) phosphatase (SaIMPase-I) in complex with the substrates D-myo-inositol-1-phosphate and NADP(+) have been solved. The structure of the SaIMPase-I-Ca(2+)-NADP(+) ternary complex reveals the catalytic mode of action of NADP(H) phosphatase. Moreover, structures of SaIMPase-I-Ca(2+)-substrate complexes have reinforced the earlier proposal that the length of the active-site-distant helix alpha4 and its preceding loop are the predisposing factors for the promiscuous substrate specificity of SaIMPase-I. Altogether, the evidence presented suggests that IMPase-family enzymes with a shorter alpha4 helix could be potential candidates for previously unreported NADP(H) phosphatase activity. Structural elucidation of the NADP(H) phosphatase activity of staphylococcal dual-specific IMPase/NADP(H) phosphatase.,Bhattacharyya S, Dutta A, Dutta D, Ghosh AK, Das AK Acta Crystallogr D Struct Biol. 2016 Feb;72(Pt 2):281-90. doi:, 10.1107/S2059798316000620. Epub 2016 Jan 28. PMID:26894675 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Inositol monophosphatase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA