MraZ from Escherichia coli: cloning, purification, crystallization and preliminary X-ray analysis
- Department of Biochemistry, Queen’s University, Kingston, Ontario K7L 3N6 (Canada)
The crystallization and preliminary X-ray diffraction analysis of MraZ, formerly known as hypothetical protein YabB, from Escherichia coli K-12 is presented. The MraZ family of proteins, also referred to as the UPF0040 family, are highly conserved in bacteria and are thought to play a role in cell-wall biosynthesis and cell division. The murein region A (mra) gene cluster encodes MraZ proteins along with a number of other proteins involved in this complex process. To date, there has been no clear functional assignment provided for MraZ proteins and the structure of a homologue from Mycoplasma pneumoniae, MPN314, failed to suggest a molecular function. The b0081 gene from Escherichia coli that encodes the MraZ protein was cloned and the protein was overexpressed, purified and crystallized. This data is presented along with evidence that the E. coli homologue exists in a different oligomeric state to the MPN314 protein.
- OSTI ID:
- 22356114
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 4; Other Information: PMCID: PMC1952425; PMID: 16511046; PUBLISHER-ID: en5105; OAI: oai:pubmedcentral.nih.gov:1952425; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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