Search Results - "Pokkuluri, P. R"

Insight into the sporulation phosphorelay: Crystal structure of the sensor domain of Bacillus subtilis histidine kinase, KinD by Wu, R., Gu, M., Wilton, R., Babnigg, G., Kim, Y., Pokkuluri, P. R., Szurmant, H., Joachimiak, A., Schiffer, M.

“…The Bacillus subtilis KinD signal‐transducing histidine kinase is a part of the sporulation phosphorelay known to regulate important developmental decisions…”
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Structures and Solution Properties of Two Novel Periplasmic Sensor Domains with c-Type Heme from Chemotaxis Proteins of Geobacter sulfurreducens: Implications for Signal Transduction by Pokkuluri, P.R., Pessanha, M., Londer, Y.Y., Wood, S.J., Duke, N.E.C., Wilton, R., Catarino, T., Salgueiro, C.A., Schiffer, M.

“…Periplasmic sensor domains from two methyl-accepting chemotaxis proteins from Geobacter sulfurreducens (encoded by genes GSU0935 and GSU0582) were expressed in…”
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Pitfalls in the interpretation of structural changes in mutant proteins from crystal structures by Pokkuluri, P. R., Yang, X., Londer, Y. Y., Schiffer, M.

“…PpcA is a small protein with 71 residues that contains three covalently bound hemes. The structures of single mutants at residue 58 have shown larger…”
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The Structure of a Mutant Photosynthetic Reaction Center Shows Unexpected Changes in Main Chain Orientations and Quinone Position by Pokkuluri, P. R, Laible, P. D, Deng, Y.-L, Wong, T. N, Hanson, D. K, Schiffer, M

“…We report on the unexpected structural changes caused by substitution of acidic amino acids in the QB binding pocket of the bacterial photosynthetic reaction…”
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Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains by RAFFEN, ROSEMARIE, DIECKMAN, LYNDA J., SZPUNAR, MEREDITH, WUNSCHL, CHRISTINE, POKKULURI, PHANI R., DAVE, PORAS, STEVENS, PRISCILLA WILKINS, CAI, XIAOYIN, SCHIFFER, MARIANNE, STEVENS, FRED J.

“…The most common form of systemic amyloidosis originates from antibody light chains. The large number of amino acid variations that distinguish amyloidogenic…”
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Structure of a novel dodecaheme cytochrome c from Geobacter sulfurreducens reveals an extended 12 nm protein with interacting hemes by Pokkuluri, P R, Londer, Y Y, Duke, N E C, Pessanha, M, Yang, X, Orshonsky, V, Orshonsky, L, Erickson, J, Zagyanskiy, Y, Salgueiro, C A, Schiffer, M

“…Multiheme cytochromes c are important in electron transfer pathways in reduction of both soluble and insoluble Fe(III) by Geobacter sulfurreducens. We…”
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A novel signal transduction protein: Combination of solute binding and tandem PAS‐like sensor domains in one polypeptide chain by Wu, R., Wilton, R., Cuff, M. E., Endres, M., Babnigg, G., Edirisinghe, J. N., Henry, C. S., Joachimiak, A., Schiffer, M., Pokkuluri, P. R.

“…We report the structural and biochemical characterization of a novel periplasmic ligand‐binding protein, Dret_0059, from Desulfohalobium retbaense DSM 5692, an…”
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Structural characterization of a family of cytochromes c(7) involved in Fe(III) respiration by Geobacter sulfurreducens by Pokkuluri, P R, Londer, Y Y, Yang, X, Duke, N E C, Erickson, J, Orshonsky, V, Johnson, G, Schiffer, M

“…Periplasmic cytochromes c(7) are important in electron transfer pathway(s) in Fe(III) respiration by Geobacter sulfurreducens. The genome of G. sulfurreducens…”
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Increasing Protein Stability by Polar Surface Residues: Domain-Wide Consequences of Interactions Within a Loop by Pokkuluri, P.R., Raffen, R., Dieckman, L., Boogaard, C., Stevens, F.J., Schiffer, M.

“…We have examined the influence of surface hydrogen bonds on the stability of proteins by studying the effects of mutations of human immunoglobulin light chain…”
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Factors contributing to decreased protein stability when aspartic acid residues are in β‐sheet regions by Pokkuluri, P.R., Gu, M., Cai, X., Raffen, R., Stevens, F.J., Schiffer, M.

“…Asp residues are significantly under represented in β‐sheet regions of proteins, especially in the middle of β‐strands, as found by a number of studies using…”
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Protein Conformation and Disease:  Pathological Consequences of Analogous Mutations in Homologous Proteins by Stevens, Fred J, Pokkuluri, Phani R, Schiffer, M

“…The antibody light chain variable domain (VL)1 and myelin protein zero (MPZ) are representatives of the functionally diverse immunoglobulin superfamily. The VL…”
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Crystallization and preliminary X-ray diffraction analysis of the glucuronoyl esterase catalytic domain from Hypocrea jecorina by Wood, S. J., Li, X.-L., Cotta, M. A., Biely, P., Duke, N. E. C., Schiffer, M., Pokkuluri, P. R.

“…The catalytic domain of the glucuronoyl esterase from Hypocrea jecorina (anamorph Trichoderma reesei) was overexpresssed, purified and crystallized by the…”
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Novel Unconventional Binding Site in the Variable Region of Immunoglobulins by Rajagopalan, Krishnan, Pavlinkova, Gabriela, Levy, Shoshana, Pokkuluri, Phani Raj, Schiffer, Marianne, Haley, Boyd E., Kohler, Heinz

“…The variable immunoglobulin (Ig) domains contain hypervariable regions that are involved in the formation of the antigen binding site. Besides the canonical…”
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A domain flip as a result of a single amino-acid substitution by Pokkuluri, PR, Huang, D-B, Raffen, R, Cai, X, Johnson, G, Stevens, P Wilkins, Stevens, FJ, Schiffer, M

“…Background: The self-assembly properties of β domains are important features of diverse classes of proteins that include cell-adhesion molecules, surface…”
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Change in dimerization mode by removal of a single unsatisfied polar residue located at the interface by POKKULURI, P.R., CAI, X., JOHNSON, G., STEVENS, F.J., SCHIFFER, M.

“…The importance of unsatisfied hydrogen bonding potential on protein–protein interaction was studied. Two alternate modes of dimerization (conventional and…”
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Outer membrane cytochrome c, OmcF, from Geobacter sulfurreducens: High structural similarity to an algal cytochrome c6 by Pokkuluri, P. R., Londer, Y. Y., Wood, S. J., Duke, N. E. C., Morgado, L., Salgueiro, C. A., Schiffer, M.

“…Putative outer membrane c-type cytochromes have been implicated in metal ion reducing properties of Geobacter sulfurreducens. OmcF (GSU2432), OmcB (GSU2731),…”
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Tertiary structure of human lambda 6 light chains by Pokkuluri, P R, Solomon, A, Weiss, D T, Stevens, F J, Schiffer, M

“…AL amyloidosis is a disease process characterized by the pathologic deposition of monoclonal light chains in tissue. To date, only limited information has been…”
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Preparation, characterization and crystallization of an antibody Fab fragment that recognizes RNA. Crystal structures of native Fab and three Fab-mononucleotide complexes by Pokkuluri, P R, Bouthillier, F, Li, Y, Kuderova, A, Lee, J, Cygler, M

“…Fab fragments from Jel 103, an antibody which specifically binds to single-stranded poly(rl), were prepared by papain digestion, separated into eight isoforms…”
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A novel signal transduction protein: Combination of solute binding and tandem PAS-like sensor domains in one polypeptide chain: Periplasmic Ligand Binding Protein Dret_0059 by Wu, R., Wilton, R., Cuff, M. E., Endres, M., Babnigg, G., Edirisinghe, J. N., Henry, C. S., Joachimiak, A., Schiffer, M., Pokkuluri, P. R.

“…We report the structural and biochemical characterization of a novel periplasmic ligand-binding protein, Dret_0059, from Desulfohalobium retbaense DSM 5692, an…”
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Structure of a novel dodecaheme cytochrome c from Geobacter sulfurreducens reveals an extended 12nm protein with interacting hemes by Pokkuluri, P.R., Londer, Y.Y., Duke, N.E.C., Pessanha, M., Yang, X., Orshonsky, V., Orshonsky, L., Erickson, J., Zagyanskiy, Y., Salgueiro, C.A., Schiffer, M.

“…Multiheme cytochromes c are important in electron transfer pathways in reduction of both soluble and insoluble Fe(III) by Geobacter sulfurreducens. We…”
Get full text