Search results for: Jhimli Dasgupta

Items from 1 to 12 out of 12 results

article

The N‐terminal FleQ domain of the Vibrio cholerae flagellar master regulator FlrA plays pivotal structural roles in stabilizing its active state

Shrestha Chakraborty, Shubhangi Agarwal, Arindam Bakshi, Sanjay Dey, more

In Vibrio cholerae, the master regulator FlrA controls transcription of downstream flagellar genes in a σ⁵⁴‐dependent manner. However, the molecular basis of regulation by VcFlrA, which contains a phosphorylation‐deficient N‐terminal FleQ domain, has remained elusive. Our studies on VcFlrA, four of its constructs, and a mutant showed that the AAA⁺ domain of VcFlrA, with or without the linker ‘L’,...

article

Purification, crystallization and preliminary X‐ray analysis of the periplasmic haem‐binding protein HutB from Vibrio cholerae

Shubhangi Agarwal, Maitree Biswas, Jhimli Dasgupta

Acta Crystallographica Section F > 71 > 4 > 401 - 404

The mechanism of haem transport across the inner membrane of pathogenic bacteria is currently insufficiently understood at the molecular level and no information is available for this process in Vibrio cholerae. To obtain structural insights into the periplasmic haem‐binding protein HutB from V. cholerae (VcHutB), which is involved in haem transport through the HutBCD haem‐transport system, at the...

article

Purification, crystallization and preliminary X‐ray analysis of the AAA⁺σ⁵⁴ activator domain of FlrC from Vibrio cholerae

Sanjay Dey, Jhimli Dasgupta

Acta Crystallographica Section F > 69 > 7 > 800 - 803

A σ⁵⁴‐dependent transcriptional activator FlrC containing an N‐terminal regulatory domain, a central AAA⁺ domain and a C‐terminal DNA‐binding domain has been implicated both in flagellar synthesis and enhanced intestinal colonization. FlrC is phosphorylated by the kinase FlrB at the regulatory domain and both nonphosphorylated and phosphorylated states of FlrC seem to be important for its functions...

article

Role of remote scaffolding residues in the inhibitory loop pre-organization, flexibility, rigidification and enzyme inhibition of serine protease inhibitors

Sudip Majumder, Susmita Khamrui, Jhimli Dasgupta, Jiban K. Dattagupta, more

BBA - Proteins and Proteomics > 2012 > 1824 > 7 > 882-890

Canonical serine protease inhibitors interact with cognate enzymes through the P3–P2′ region of the inhibitory loop while its scaffold hardly makes any contact. Neighboring scaffolding residues like Arginines or Asparagine shape-up the inhibitory loop and favor the resynthesis of cleaved scissile bond. However, role of remote scaffolding residues, which are not involved in religation, was not properly...

article

Overexpression, purification, crystallization and preliminary X‐ray analysis of CheY4 from Vibrio cholerae O395

Maitree Biswas, Susmita Khamrui, Udayaditya Sen, Jhimli Dasgupta

Acta Crystallographica Section F > 67 > 12 > 1645 - 1648

Chemotaxis and motility greatly influence the infectivity of Vibrio cholerae, although the role of chemotaxis genes in V. cholerae pathogenesis is poorly understood. In contrast to the single copy of CheY found in Escherichia coli and Salmonella typhimurium, four CheYs (CheY1–CheY4) are present in V. cholerae. While insertional disruption of the cheY4 gene results in decreased motility, insertional...

article

Cloning, overexpression, purification, crystallization and preliminary X‐ray analysis of CheY3, a response regulator that directly interacts with the flagellar `switch complex' in Vibrio cholerae

Susmita Khamrui, Maitree Biswas, Udayaditya Sen, Jhimli Dasgupta

Acta Crystallographica Section F > 66 > 8 > 944 - 947

Vibrio cholerae is the aetiological agent of the severe diarrhoeal disease cholera. This highly motile organism uses the processes of motility and chemotaxis to travel and colonize the intestinal epithelium. Chemotaxis in V. cholerae is far more complex than that in Escherichia coli or Salmonella typhimurium, with multiple paralogues of various chemotaxis genes. In contrast to the single copy of the...

article

Crystal Structure of the Human Lymphoid Tyrosine Phosphatase Catalytic Domain: Insights into Redox Regulation,

Sophia J. Tsai, Udayaditya Sen, Lei Zhao, William B. Greenleaf, more

Biochemistry > 2009 > 48 > 22 > 4838 - 4845

article

Analysis of specificity determinants in the interactions of different HPV E6 proteins with their PDZ domain-containing substrates

Miranda Thomas, Jhimli Dasgupta, Yi Zhang, Xiaojiang Chen, more

Virology > 2008 > 376 > 2 > 371-378

The E6 oncoproteins of the cancer-associated human papillomaviruses (high-risk HPV types) characteristically have a PDZ-binding motif at their extreme carboxy-termini. However, they interact with only some of the PDZ domain-containing proteins in the human proteome and, despite many of these proteins having multiple PDZ domains, they interact specifically through only one of those domains. Previous...

article

Spacer Asn Determines the Fate of Kunitz (STI) Inhibitors, as Revealed by Structural and Biochemical Studies on WCI Mutants ^‡

Jhimli Dasgupta, Susmita Khamrui, Jiban K. Dattagupta, Udayaditya Sen

Biochemistry > 2006 > 45 > 22 > 6783 - 6792

article

Single mutation at P1 of a chymotrypsin inhibitor changes it to a trypsin inhibitor: X-ray structural (2.15 Å) and biochemical basis

Susmita Khamrui, Jhimli Dasgupta, Jiban K. Dattagupta, Udayaditya Sen

BBA - Proteins and Proteomics > 2005 > 1752 > 1 > 65-72

Change in specificity, caused by the mutations at P1 site, of the serine protease inhibitors of different families is reported in the literature, but Kunitz (STI) family inhibitors are almost unexplored in this regard. In this paper, we present the crystal structure of a P1 variant of winged bean chymotrypsin inhibitor (WCI) belonging to Kunitz (STI) family, supplemented by biochemical, phylogenetic...

article

Crystal Structures of HbA ₂ and HbE and Modeling of Hemoglobin δ ₄ : Interpretation of the Thermal Stability and the Antisickling Effect of HbA ₂ and Identification of the Ferrocyanide Binding Site in Hb ^‡

Udayaditya Sen, Jhimli Dasgupta, Debi Choudhury, Poppy Datta, more

Biochemistry > 2004 > 43 > 39 > 12477 - 12488

article

Crystallization and preliminary X-ray structural studies of hemoglobin A ₂ and hemoglobin E, isolated from the blood samples of β-thalassemic patients

Jhimli Dasgupta, Udayaditya Sen, Debi Choudhury, Poppy Datta, more

Biochemical and Biophysical Research Communications > 2003 > 303 > 2 > 619-623

Hemoglobin A ₂ (α ₂ δ ₂ ), a minor (2-3%) component of circulating red blood cells, acts as an anti-sickling agent and its elevated concentration in β-thalassemia is a useful clinical diagnostic. In β-thalassemia major, where there is a failure of β-chain production, HbA ₂ acts as the predominant oxygen deliverer. Hemoglobin E, is another common abnormal hemoglobin,...

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Search results for: Jhimli Dasgupta

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