The Prototypical Young L/T-Transition Dwarf HD 203030B Likely Has Planetary Mass

Upon its discovery in 2006, the young L7.5 companion to the solar analog HD 203030 was found to be unusual in being $\approx$200 K cooler than older late-L dwarfs. HD 203030B offered the first clear indication that the effective temperature at the L-to-T spectral type transition depends on surface gravity: now a well-known characteristic of low-gravity ultra-cool dwarfs. An initial age analysis of the G8V primary star indicated that the system was 130--400 Myr old, and so the companion between 12--31 $M_{\rm Jup}$. Using moderate resolution near-infrared spectra of HD 203030B, we now find features of very low gravity comparable to those of 10--150 Myr-old L7--L8 dwarfs. We also obtained more accurate near infrared and {\sl Spitzer}/IRAC photometry, and find a $(J-K)_{\rm MKO}$ color of $2.56\pm0.13$ mag---comparable to those observed in other young planetary-mass objects---and a luminosity of log($L_{\rm bol}/L_{\odot}$)$\,=\,-4.75\pm0.04$ dex. We further reassess the evidence for the young age of the host star, HD 203030, with a more comprehensive analysis of the photometry and updated stellar activity measurements and age calibrations. Summarizing the age diagnostics for both components of the binary, we adopt an age of 100 Myr for HD 203030B and an age range of 30--150 Myr. Using cloudy evolutionary models, the new companion age range and luminosity result in a mass of 11 $M_{\rm Jup}$ with a range of 8--15 $M_{\rm Jup}$, and an effective temperature of $1040\pm50$ K.Comment: 12 pages, 7 figures, accepted for publication in A

Crystal sructure of photorespiratory alanine: Glyoxylate aminotransferase 1 (AGT1) from \u3ci\u3eArabidopsis thaliana\u3c/i\u3e

Photorespiration is an energetically costly metabolic pathway for the recycling of phosphoglycolate produced by the oxygenase activity of ribulose-1,5-bisphosphate carboxylase/oxygenase (RUBISCO) to phosphoglycerate. Arabidopsis alanine:glyoxylate aminotransferase 1 (AGT1) is a peroxisomal aminotransferase with a central role in photorespiration. This enzyme catalyzes various aminotransferase reactions, including serine:glyoxylate, alanine:glyoxylate, and asparagine:glyoxylate transaminations. To better understand structural features that govern the specificity of this enzyme, its crystal structures in the native form (2.2-Å resolution) and in the presence of l-serine (2.1-Å resolution) were solved. The structures confirm that this enzyme is dimeric, in agreement with studies of the active enzyme in solution. In the crystal, another dimer related by noncrystallographic symmetry makes close interactions to form a tetramer mediated in part by an extra carboxyl-terminal helix conserved in plant homologs of AGT1. Pyridoxal 5′-phosphate (PLP) is bound at the active site but is not held in place by covalent interactions. Residues Tyr35′ and Arg36′, entering the active site from the other subunits in the dimer, mediate interactions between AGT and l-serine when used as a substrate. In comparison, AGT1 from humans and AGT1 from Anabaena lack these two residues and instead position a tyrosine ring into the binding site, which accounts for their preference for l-alanine instead of l-serine. The structure also rationalizes the phenotype of the sat mutant, Pro251 to Leu, which likely affects the dimer interface near the catalytic site. This structural model of AGT1 provides valuable new information about this protein that may enable improvements to the efficiency of photorespiration