This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Nature has given us a tremendous amount of structurally diverse natural products which we use to combat diseases ranging from the common cold to cancer. The question of how bacteria and other organisms make these compounds needs to be investigated. We are investigating several proteins that have very interesting activity in their biosynthetic pathways. LnmQ is an adenylation domain in the leinamycin biosynthetic pathway which specifically activates D-Ala. This is the only known adenylation domain to be specific for the unnatural stereoisomer. This proposal will use the technique of X-ray crystallography to determine exactly how this enzyme works mechanistically and how it can recognize a small hydrophobic side chain such as that of D-Ala. Native and Se-Met crystals have been grown for this protein. They have been screened at our home source and we have been able to get information regarding space group and unit cell dimensions. LnmQ has a space group of C2 and a unit cell of a=97.714, b=102.412, c=79.008 with } =90, } =116.973, } =90.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR012408-11
Application #
7602329
Study Section
Special Emphasis Panel (ZRG1-PC (02))
Project Start
2007-07-01
Project End
2008-06-30
Budget Start
2007-07-01
Budget End
2008-06-30
Support Year
11
Fiscal Year
2007
Total Cost
$3,372
Indirect Cost
Name
Brookhaven National Laboratory
Department
Type
DUNS #
027579460
City
Upton
State
NY
Country
United States
Zip Code
11973
Sui, Xuewu; Farquhar, Erik R; Hill, Hannah E et al. (2018) Preparation and characterization of metal-substituted carotenoid cleavage oxygenases. J Biol Inorg Chem 23:887-901
Jacques, Benoit; Coinçon, Mathieu; Sygusch, Jurgen (2018) Active site remodeling during the catalytic cycle in metal-dependent fructose-1,6-bisphosphate aldolases. J Biol Chem 293:7737-7753
Fuller, Franklin D; Gul, Sheraz; Chatterjee, Ruchira et al. (2017) Drop-on-demand sample delivery for studying biocatalysts in action at X-ray free-electron lasers. Nat Methods 14:443-449
Wangkanont, Kittikhun; Winton, Valerie J; Forest, Katrina T et al. (2017) Conformational Control of UDP-Galactopyranose Mutase Inhibition. Biochemistry 56:3983-3992
VanderLinden, Ryan T; Hemmis, Casey W; Yao, Tingting et al. (2017) Structure and energetics of pairwise interactions between proteasome subunits RPN2, RPN13, and ubiquitin clarify a substrate recruitment mechanism. J Biol Chem 292:9493-9504
Song, Lingshuang; Yang, Lin; Meng, Jie et al. (2017) Thermodynamics of Hydrophobic Amino Acids in Solution: A Combined Experimental-Computational Study. J Phys Chem Lett 8:347-351
Orlova, Natalia; Gerding, Matthew; Ivashkiv, Olha et al. (2017) The replication initiator of the cholera pathogen's second chromosome shows structural similarity to plasmid initiators. Nucleic Acids Res 45:3724-3737
Firestone, Ross S; Cameron, Scott A; Karp, Jerome M et al. (2017) Heat Capacity Changes for Transition-State Analogue Binding and Catalysis with Human 5'-Methylthioadenosine Phosphorylase. ACS Chem Biol 12:464-473
Guo, Bingqian; McMillan, Brian J; Blacklow, Stephen C (2016) Structure and function of the Mind bomb E3 ligase in the context of Notch signal transduction. Curr Opin Struct Biol 41:38-45
Simmons, Chad R; Zhang, Fei; Birktoft, Jens J et al. (2016) Construction and Structure Determination of a Three-Dimensional DNA Crystal. J Am Chem Soc 138:10047-54

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