1HZ4

CRYSTAL STRUCTURE OF TRANSCRIPTION FACTOR MALT DOMAIN III

Summary for 1HZ4

• Entry DOI: 10.2210/pdb1hz4/pdb
• Descriptor: MALT REGULATORY PROTEIN, SULFATE ION, BENZOIC ACID, ... (5 entities in total)
• Functional Keywords: two-helix bundles, helix repeats, protein superhelix, transcription activator
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 43998.46

Authors

Steegborn, C.,Danot, O.,Clausen, T.,Huber, R. (deposition date: 2001-01-23, release date: 2001-11-28, Last modification date: 2024-02-07)

Primary citation

Steegborn, C.,Danot, O.,Huber, R.,Clausen, T.
Crystal structure of transcription factor MalT domain III: a novel helix repeat fold implicated in regulated oligomerization.
Structure, 9:1051-1060, 2001

PubMed Abstract: MalT from Escherichia coli, the best-studied member of the MalT family of ATP-dependent transcriptional activators, regulates the genes for malto-oligosaccharide utilization. The active form of this 4 domain protein is a homooligomer, and its multimerization is induced by the binding of maltotriose. Domains II and III of MalT were suggested to mediate the oligomerization process, but its molecular mechanism and the specific functions of these domains remain to be identified.

PubMed: 11709169
DOI: 10.1016/S0969-2126(01)00665-7

Experimental method

X-RAY DIFFRACTION (1.45 Å)