4RSM

Crystal structure of carbohydrate transporter msmeg_3599 from mycobacterium smegmatis str. mc2 155, target efi-510970, in complex with d-threitol

Summary for 4RSM

• Entry DOI: 10.2210/pdb4rsm/pdb
• Descriptor: Periplasmic binding protein/LacI transcriptional regulator, D-Threitol (3 entities in total)
• Functional Keywords: sugar transporter, abc-type, enzyme function initiative, efi, structural genomics, transport protein, hydrolase
• Biological source: Mycobacterium smegmatis
• Cellular location: Cell membrane ; Lipid-anchor : A0QYB5
• Total number of polymer chains: 4
• Total formula weight: 137874.78

Authors

Patskovsky, Y.,Toro, R.,Bhosle, R.,Al Obaidi, N.,Morisco, L.L.,Wasserman, S.R.,Chamala, S.,Attonito, J.D.,Scott Glenn, A.,Chowdhury, S.,Lafleur, J.,Hillerich, B.,Siedel, R.D.,Love, J.,Whalen, K.L.,Gerlt, J.A.,Almo, S.C.,Enzyme Function Initiative (EFI) (deposition date: 2014-11-08, release date: 2014-12-10, Last modification date: 2024-02-28)

Primary citation

Huang, H.,Carter, M.S.,Vetting, M.W.,Al-Obaidi, N.,Patskovsky, Y.,Almo, S.C.,Gerlt, J.A.
A General Strategy for the Discovery of Metabolic Pathways: d-Threitol, l-Threitol, and Erythritol Utilization in Mycobacterium smegmatis.
J.Am.Chem.Soc., 137:14570-14573, 2015

PubMed Abstract: We describe a general integrated bioinformatic and experimental strategy to discover the in vitro enzymatic activities and in vivo functions (metabolic pathways) of uncharacterized enzymes discovered in microbial genome projects using the ligand specificities of the solute binding proteins (SBPs) for ABC transporters. Using differential scanning fluorimetry, we determined that the SBP for an ABC transporter encoded by the genome of Mycobacterium smegmatis is stabilized by d-threitol. Using sequence similarity networks and genome neighborhood networks to guide selection of target proteins for pathway enzymes, we applied both in vitro and in vivo experimental approaches to discover novel pathways for catabolism of d-threitol, l-threitol, and erythritol.

PubMed: 26560079
DOI: 10.1021/jacs.5b08968

Experimental method

X-RAY DIFFRACTION (1.6 Å)