Pavel P KhilSummaryAffiliation: National Institutes of Health Country: USA Publications
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Detail Information
Publications
Crystal structure of Escherichia coli protein ybgI, a toroidal structure with a dinuclear metal siteJane E Ladner
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, MD 20850, USA
BMC Struct Biol 3:7. 2003..The protein encoded by the gene ybgI was chosen as a target for a structural genomics project emphasizing the relation of protein structure to function...
Crystal structure of the Escherichia coli YjiA protein suggests a GTP-dependent regulatory functionPavel P Khil
Genetics and Biochemistry Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA
Proteins 54:371-4. 2004
Crystal structure of the YgfZ protein from Escherichia coli suggests a folate-dependent regulatory role in one-carbon metabolismAlexey Teplyakov
Center for Advanced Research in Biotechnology, 9600 Gudelsky Drive, Rockville, MD 20850, USA
J Bacteriol 186:7134-40. 2004....
Crystal structure of the Escherichia coli Tas protein, an NADP(H)-dependent aldo-keto reductaseGalina Obmolova
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, Rockville, Maryland 20850, USA
Proteins 53:323-5. 2003
Crystal structure of the YchF protein reveals binding sites for GTP and nucleic acidAlexey Teplyakov
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, Rockville, Maryland 20850, USA
J Bacteriol 185:4031-7. 2003..Taken together with other experimental data and genomic analysis, these results suggest that YchF may be part of a nucleoprotein complex and may function as a GTP-dependent translation factor...
Crystal structure of the Escherichia coli YcdX protein reveals a trinuclear zinc active siteAlexey Teplyakov
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, Rockville, Maryland 20850, USA
Proteins 51:315-8. 2003
Crystal structure of the YajQ protein from Haemophilus influenzae reveals a tandem of RNP-like domainsAlexey Teplyakov
Center for Advanced Research in Biotechnology of the University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, MD 20850, USA
J Struct Funct Genomics 4:1-9. 2003..This structural motif is a characteristic feature of many RNA-binding proteins. The tetrameric structure observed in the crystal suggests a possibility of binding two stretches of double-stranded nucleic acid...
Assisting functional assignment for hypothetical Heamophilus influenzae gene products through structural genomicsGary L Gilliland
Center for Advanced Research in Biotechnology of the University of Maryland Biotechnology Institute and the National Institute of Standards and Technology, 9600 Gudelsky Drive, Rockville, MD 20850, USA
Curr Drug Targets Infect Disord 2:339-53. 2002..In addition to aiding in functional assignment, this effort is identifying a number of possible new targets for drug development...
Crystal structure of the YffB protein from Pseudomonas aeruginosa suggests a glutathione-dependent thiol reductase functionAlexey Teplyakov
Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, 9600 Gudelsky Drive, Rockville, MD 20850, USA
BMC Struct Biol 4:5. 2004..The crystal structure determination of YffB was undertaken as part of a structural genomics effort in order to assist with the functional assignment of the protein...
Crystal structure of the YjeE protein from Haemophilus influenzae: a putative Atpase involved in cell wall synthesisAlexey Teplyakov
Center for Advanced Research in Biotechnology of the University of Maryland Biotechnology Institute, Rockville, Maryland 20850, USA
Proteins 48:220-6. 2002..The distribution of conserved residues suggests that the protein may work as a "molecular switch" triggered by ATP hydrolysis. The phylogenetic pattern of YjeE suggests its involvement in cell wall biosynthesis...
