Crystal Structures of Mycobacterium smegmatis RecA and Its Nucleotide Complexes (original) (raw)

Snapshots of RecA Protein Involving Movement of the C-domain and Different Conformations of the DNA-binding Loops: Crystallographic and Comparative Analysis of 11 Structures of Mycobacterium smegmatis RecA

Nagasuma Chandra

Journal of Molecular Biology, 2007

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Structure of Mycobacterium smegmatis single-stranded DNA-binding protein and a comparative study involving homologus SSBs: biological implications of structural plasticity and variability in quaternary association

Pawan Singh

Acta Crystallographica Section D-biological Crystallography, 2005

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Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AlF4: implications for decreased ATPase activity and molecular aggregation

Moses Prabu

Nucleic Acids Research, 2000

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Structural Studies on the Second Mycobacterium smegmatis Dps: Invariant and Variable Features of Structure, Assembly and Function

S Roy

Journal of Molecular Biology, 2008

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Crystallographic and solution structure of the N-terminal domain of the Rel protein fromMycobacterium tuberculosis

Jeyaraman Jeyakanthan

FEBS Letters, 2017

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The crystal structure of the single-stranded DNA-binding protein from Mycobacterium tuberculosis

Jeyaraman Jeyakanthan

Acta Crystallographica Section A Foundations of Crystallography, 2002

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Structure of Mycobacterium tuberculosis Single-stranded DNA-binding Protein. Variability in Quaternary Structure and Its Implications

Narottam Acharya

Journal of Molecular Biology, 2003

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Plasticity, ligand conformation and enzyme action of Mycobacterium smegmatis MutT1

Karthik Selvam

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X-ray Analysis of Mycobacterium smegmatis Dps and a Comparative Study Involving Other Dps and Dps-like Molecules

surbhi gupta

Journal of Molecular Biology, 2004

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Crystallographic identification of an ordered C-terminal domain and a second nucleotide-binding site in RecA: new insights into allostery

Nagasuma Chandra

Nucleic Acids Research, 2006

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Mycobacterium leprae RecA is structurally analogous but functionally distinct from Mycobacterium tuberculosis RecA protein

Sri Harsha

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2011

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The crystal structure of Mycobacterium tuberculosis NrdH at 0.87 Å suggests a possible mode of its activity

Shekhar Mande

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Structural analysis reveals DNA binding properties of Rv2827c, a hypothetical protein from Mycobacterium tuberculosis

santosh Panjikar

Journal of Structural and Functional Genomics, 2009

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DNA Binding, Coprotease, and Strand Exchange Activities of Mycobacterial RecA Proteins: Implications for Functional Diversity among RecA Nucleoprotein Filaments

pawan Singh

Biochemistry, 2011

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The Three-dimensional Structure of a Mycobacterial DapD Provides Insights into DapD Diversity and Reveals Unexpected Particulars about the Enzymatic Mechanism

Simone Weyand

Journal of Molecular Biology, 2009

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Role of N and C-terminal Tails in DNA Binding and Assembly in Dps: Structural Studies of Mycobacterium smegmatis Dps Deletion Mutants

Surbhi Gupta

Journal of Molecular Biology, 2007

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Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

Arockiasamy Arulandu

Proceedings of The National Academy of Sciences, 2003

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Structure of the DNA-Binding Domain of the Response Regulator PhoP from Mycobacterium tuberculosis † , ‡

Issar Smith

Biochemistry, 2007

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Mycobacterium tuberculosis RecG binds and unwinds model DNA substrates with a preference for Holliday junctions

Ephrem Debebe

Microbiology, 2012

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Evidence for nucleotide-mediated changes in the domain structure of the RecA protein of Escherichia coli

Kendall Knight

Biochemistry, 1987

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Crystallization and preliminary crystallographic analysis of the putative sugar-binding protein Msmeg_0515 (AgaE) from Mycobacterium smegmatis

Feras Almourfi

Acta crystallographica. Section F, Structural biology communications, 2015

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Structure of Mycobacterium tuberculosis RuvA, a protein involved in recombination

Brent Segelke

Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2006

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