How ATPases unravel a mystery

Nerea Gallastegui; Michael Groll

doi:10.1016/j.str.2009.09.003

How ATPases unravel a mystery

Structure. 2009 Oct 14;17(10):1279-81. doi: 10.1016/j.str.2009.09.003.

Authors

Nerea Gallastegui¹, Michael Groll

Affiliation

¹ Center for Integrated Protein Science, Department Chemie, Lehrstuhl für Biochemie, Technische Universität München, Lichtenbergstrasse 4, Garching, Germany.

PMID: 19836328
DOI: 10.1016/j.str.2009.09.003

Abstract

Principles of intracellular protein degradation remain among the most challenging questions in cell biology. Here, we discuss Wang and colleagues' crystal structure elucidation of the intermediate domain of Mpa, a regulatory particle of Mtb proteasome, the core proteolytic machinery of Mycobacterium tuberculosis.

Publication types

Comment

MeSH terms

Adenosine Triphosphatases / chemistry*
Adenosine Triphosphatases / metabolism
Bacterial Proteins / chemistry*
Bacterial Proteins / metabolism
Models, Molecular
Mycobacterium tuberculosis / enzymology*
Mycobacterium tuberculosis / metabolism
Proteasome Endopeptidase Complex / metabolism
Protein Conformation
Protein Folding

Substances

Bacterial Proteins
Proteasome Endopeptidase Complex
Adenosine Triphosphatases
Mpa protein, Mycobacterium tuberculosis