Author

B. A. Kelch

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 10 Biophysics· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 12 Research Focus:chromatin & epigenetic regulation· 5 Assay:cryo-EM· 5 Research Focus:protein folding & dynamics· 4 Research Focus:protein structure prediction· 4 Approach:statistical model· 3 Assay:structural biology· 3 Organism:bacteria (other)· 2

Frequent Co-Authors

C. Gaubitz· 5 shared J. Pajak· 5 shared N. P. Stone· 5 shared B. J. Hilbert· 4 shared X. Liu· 4 shared E. Agnello· 3 shared J. A. Hayes· 3 shared G. Demo· 2 shared

Activity by Year

2016-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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5 shared papersBiochemistry

C. Gaubitz

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Author profile →

13 papers

Recent·Most cited

Differences in clamp loader mechanism between bacteria and eukaryotes

J. T. Landeck, J. Pajak, E. K. Norman, E. L. Sedivy, B. A. Kelch

This study compares the clamp loader mechanism in bacteria and eukaryotes, revealing structural and functional differences in clamp opening and p/t-junction binding.

bioRxiv · Nov 30, 2023 · PreprintBiochemistry

Structure and assembly of an extremely long bacteriophage tail tube

E. Agnello, J. Pajak, X. Liu, B. A. Kelch

This study presents the structure of the P74-26 bacteriophage tail tube and proposes a model for its assembly mechanism based on cryo-EM data and complementary experiments.

bioRxiv · Oct 3, 2022 · PreprintBiophysics

A second DNA binding site on RFC facilitates clamp loading at gapped or nicked DNA

X. Liu, C. Gaubitz, J. Pajak, B. A. Kelch

This paper identifies a second DNA binding site in yeast RFC that facilitates clamp loading at nicked or gapped DNA, enhancing DNA repair processes.

bioRxiv · Jan 31, 2022Biochemistry

Cryo-EM structures reveal high-resolution mechanism of a DNA polymerase sliding clamp loader

C. Gaubitz, X. Liu, J. Pajak, N. P. Stone, J. A. Hayes, G. Demo, B. A. Kelch

The paper presents cryo-EM structures of the yeast clamp loader RFC bound to PCNA, revealing the mechanism of clamp opening and DNA binding without ATP hydrolysis.

bioRxiv · Sep 23, 2021Biochemistry

Viral Packaging ATPases Utilize a Glutamate Switch to Couple ATPase Activity and DNA Translocation

J. Pajak, R. Atz, B. J. Hilbert, M. Morais, B. A. Kelch, P. Jardine, G. Arya

This study identifies a glutamate switch mechanism in viral packaging ATPases that couples ATP binding to DNA translocation through conformational changes.

bioRxiv · Dec 1, 2020Biophysics

CaMKII binds both substrates and activators at the active site

C. Ozden, R. Sloutsky, T. Mitsugi, N. Santos, E. Agnello, C. Gaubitz, J. Foster, E. Lapinskas, E. A. Esposito, T. Saneyoshi, B. A. Kelch, S. C. Garman, Y. Hayashi, M. Stratton

This study challenges a longstanding model of CaMKII activation by showing that activators and substrates bind to a single site rather than distinct S- and T-sites.

bioRxiv · Oct 25, 2020Biochemistry

Exploring the evolutionary history of kinetic stability in the alpha-lytic protease family

C. F. Nixon, S. A. Lim, Z. R. Sailer, I. N. Zheludev, C. L. Gee, B. A. Kelch, M. J. Harms, S. Marqusee

This study investigates how sequence variation in the alpha-lytic protease family relates to kinetic stability and energy landscapes, finding that pro-region size and specific amino acids influence folding speed and stability.

bioRxiv · Aug 30, 2020Biophysics

Structure of the human clamp loader bound to the sliding clamp: a further twist on AAA+ mechanism

C. Gaubitz, X. Liu, J. Magrino, N. P. Stone, J. Landeck, M. Hedglin, B. A. Kelch

This paper reports the cryo-EM structure of human RFC bound to PCNA, revealing an autoinhibited conformation and a novel regulatory mechanism for AAA+ ATPases.

bioRxiv · Feb 18, 2020Biochemistry

A thermophilic phage uses a small terminase protein with a fixed helix-turn-helix geometry

J. A. Hayes, B. J. Hilbert, C. Gaubitz, N. P. Stone, B. A. Kelch

This paper identifies and characterizes the TerS protein of bacteriophage P74-26, revealing its unique structural features and functional roles in DNA binding and TerL interaction.

bioRxiv · Nov 21, 2019Biochemistry

Principles for enhancing virus capsid capacity and stability from a thermophilic virus capsid structure

N. Stone, G. Demo, E. Agnello, B. A. Kelch

The paper determines the structure of a thermostable virus capsid and identifies structural features that enhance stability and capacity.

bioRxiv · Jan 5, 2019Biochemistry

A hyperthermophilic phage decoration protein suggests common evolutionary origin with Herpesvirus Triplex proteins and an anti-CRISPR protein

N. P. Stone, B. J. Hilbert, D. Hidalgo, K. T. Halloran, B. A. Kelch

The paper investigates the structure and stability of a capsid protein from a hyperthermophilic phage, revealing its evolutionary relationship with herpesvirus triplex proteins and an anti-CRISPR protein.

bioRxiv · Nov 13, 2017Biochemistry

Substrate sequence selectivity of APOBEC3A implicates intra-DNA interactions

T. V. Silvas, S. Hou, W. Myint, M. Somasundaran, B. A. Kelch, H. Matsuo, N. Kurt Yilmaz, C. A. Schiffer

This study identifies the APOBEC3A ssDNA binding motif and shows that substrate affinity is influenced by DNA structure, not just sequence, leading to a new model for its sequence preference.

bioRxiv · Aug 17, 2017Biochemistry

The large terminase DNA packaging motor grips DNA with its ATPase domain for cleavage by the flexible nuclease domain

B. J. Hilbert, J. A. Hayes, N. P. Stone, R.-G. Xu, B. A. Kelch

This study investigates how the large terminase protein binds and cleaves DNA during viral genome packaging, revealing the ATPase domain's role in DNA binding and the nuclease domain's role in cleavage.

bioRxiv · Oct 19, 2016Biochemistry