5m8h

ATP phosphoribosyltransferase (HisZG ATPPRT) from Psychrobacter arcticus

spinqualitylabelsall models 5m8h, resolution 2.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5m8h is a 8 chain structure with sequence from Psychrobacter arcticus 273-4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.34Å Ligands: CL, MPD, SR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HISZ_PSYA2 Required for the first step of histidine biosynthesis. May allow the feedback regulation of ATP phosphoribosyltransferase activity by histidine.[HAMAP-Rule:MF_00125] Publication Abstract from PubMed Adenosine 5'-triphosphate phosphoribosyltransferase (ATPPRT) catalyzes the first step in histidine biosynthesis, the condensation of ATP and 5-phospho-alpha-d-ribosyl-1-pyrophosphate to generate N1-(5-phospho-beta-d-ribosyl)-ATP and inorganic pyrophosphate. The enzyme is allosterically inhibited by histidine. Two forms of ATPPRT, encoded by the hisG gene, exist in nature, depending on the species. The long form, HisGL, is a single polypeptide chain with catalytic and regulatory domains. The short form, HisGS, lacks a regulatory domain and cannot bind histidine. HisGS instead is found in complex with a regulatory protein, HisZ, constituting the ATPPRT holoenzyme. HisZ triggers HisGS catalytic activity while rendering it sensitive to allosteric inhibition by histidine. Until recently, HisGS was thought to be catalytically inactive without HisZ. Here, recombinant HisGS and HisZ from the psychrophilic bacterium Psychrobacter arcticus were independently overexpressed and purified. The crystal structure of P. arcticus ATPPRT was determined at 2.34 A resolution, revealing an equimolar HisGS-HisZ hetero-octamer. Steady-state kinetics indicate that both the ATPPRT holoenzyme and HisGS are catalytically active. Surprisingly, HisZ confers only a modest 2-4-fold increase in kcat. Reaction profiles for both enzymes cannot be distinguished by 31P nuclear magnetic resonance, indicating that the same reaction is catalyzed. The temperature dependence of kcat shows deviation from Arrhenius behavior at 308 K with the holoenzyme. Interestingly, such deviation is detected only at 313 K with HisGS. Thermal denaturation by CD spectroscopy resulted in Tm's of 312 and 316 K for HisZ and HisGS, respectively, suggesting that HisZ renders the ATPPRT complex more thermolabile. This is the first characterization of a psychrophilic ATPPRT. Kinetics and Structure of a Cold-Adapted Hetero-Octameric ATP Phosphoribosyltransferase.,Stroek R, Ge Y, Talbot PD, Glok MK, Bernas KE, Thomson CM, Gould ER, Alphey MS, Liu H, Florence GJ, Naismith JH, da Silva RG Biochemistry. 2017 Feb 7;56(5):793-803. doi: 10.1021/acs.biochem.6b01138. Epub, 2017 Jan 24. PMID:28092443 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATP phosphoribosyl transferase 3D structures

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