Structural model of the full-length Ser/Thr protein kinase StkP from S. pneumoniae and its recognition of peptidoglycan fragments-Reference-Cited by-同舟云学术

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Structural model of the full-length Ser/Thr protein kinase StkP from S. pneumoniae and its recognition of peptidoglycan fragments

Published:2017-11-07 Issue:14 Volume:36 Page:3666-3679
ISSN:0739-1102
Container-title:Journal of Biomolecular Structure and Dynamics
language:en
Short-container-title:Journal of Biomolecular Structure and Dynamics

Author:

Righino Benedetta¹,Galisson Frédéric²,Pirolli Davide¹³,Vitale Serena¹,Réty Stéphane²,Gouet Patrice²,De Rosa Maria Cristina³

Affiliation:

1. Istituto di Biochimica e Biochimica Clinica, Università Cattolica del Sacro Cuore, L.go F. Vito 1, Rome 00168, Italy

2. Molecular Microbiology and Structural Biochemistry Institute, UMR5086 CNRS Univ-Lyon, Cedex 7, Lyon F-69367, France

3. Istituto di Chimica del Riconoscimento Molecolare (ICRM), CNR c/o Università Cattolica del Sacro Cuore L.go F, Vito 1, Rome 00168, Italy

Publisher

Informa UK Limited

Subject

Molecular Biology,General Medicine,Structural Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/07391102.2017.1395767

Reference59 articles.

1. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

2. No longer an exclusive club: eukaryotic signalling domains in bacteria

3. ProDy: Protein Dynamics Inferred from Theory and Experiments

4. The Structure of PknB Extracellular PASTA Domain from Mycobacterium tuberculosis Suggests a Ligand-Dependent Kinase Activation

5. Control of cell division in Streptococcus pneumoniae by the conserved Ser/Thr protein kinase StkP

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