6pc3 | pdb_00006pc3

Crystal structure of Helicobacter pylori PPX/GppA in complex with GSP

spinqualitylabelsall models 6pc3, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6pc3 is a 2 chain structure with sequence from Helicobacter pylori G27. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: CL, EDO, GSP, K, MG, PO4, TS6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B5ZA44_HELPG Publication Abstract from PubMed Rapid adaptation to environmental changes is crucial for bacterial survival. Almost all bacteria possess a conserved stringent response system to prompt transcriptional and metabolic responses toward stress. The adaptive process relies on alarmones, guanosine pentaphosphate (pppGpp) and tetraphosphate (ppGpp), to regulate global gene expression. The ppGpp is more potent than pppGpp in the regulatory activity and pppGpp phosphohydrolase (GppA) plays a key role in (p)ppGpp homeostasis. Sharing a similar domain structure, GppA is indistinguishable from exopolyphosphatase (PPX), which mediates the metabolism of cellular inorganic polyphosphate. Here, our phylogenetic analysis of PPX/GppA homologs in bacteria shows a wide distribution with several distinct subfamilies, and our structural and functional analysis of Escherichia coli GppA and Helicobacter pylori PPX/GppA reveals unique properties of each homolog. These results explain how each homolog possesses its distinct functionality. Structure and Activity of PPX/GppA Homologs from Escherichia coli and Helicobacter pylori.,Song H, Dharmasena MN, Wang C, Shaw GX, Cherry S, Tropea JE, Jin DJ, Ji X FEBS J. 2019 Nov 2. doi: 10.1111/febs.15120. PMID:31679177 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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