5D9R

Crystal structure of a conserved domain in the intermembrane space region of the plastid division protein ARC6

Summary for 5D9R

• Entry DOI: 10.2210/pdb5d9r/pdb
• Descriptor: Protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS 6, chloroplastic (2 entities in total)
• Functional Keywords: plastid division machinery, biosynthetic protein
• Biological source: Arabidopsis thaliana (Mouse-ear cress)
• Cellular location: Plastid, chloroplast inner membrane ; Single- pass membrane protein : Q9FIG9
• Total number of polymer chains: 1
• Total formula weight: 20522.01

Authors

Radhakrishnan, A.,Kumar, N.,Su, C.-C.,Chou, T.-H.,Yu, E. (deposition date: 2015-08-18, release date: 2015-11-11, Last modification date: 2024-03-06)

Primary citation

Kumar, N.,Radhakrishnan, A.,Su, C.C.,Osteryoung, K.W.,Yu, E.W.
Crystal structure of a conserved domain in the intermembrane space region of the plastid division protein ARC6.
Protein Sci., 25:523-529, 2016

PubMed Abstract: The chloroplast division machinery is composed of numerous proteins that assemble as a large complex to divide double-membraned chloroplasts through binary fission. A key mediator of division-complex formation is ARC6, a chloroplast inner envelope protein and evolutionary descendant of the cyanobacterial cell division protein Ftn2. ARC6 connects stromal and cytosolic contractile rings across the two membranes through interaction with an outer envelope protein within the intermembrane space (IMS). The ARC6 IMS region bears a structurally uncharacterized domain of unknown function, DUF4101, that is highly conserved among ARC6 and Ftn2 proteins. Here we report the crystal structure of this domain from Arabidopsis thaliana ARC6. The domain forms an α/β barrel open towards the outer envelope membrane but closed towards the inner envelope membrane. These findings provide new clues into how ARC6 and its homologs contribute to chloroplast and cyanobacterial cell division.

PubMed: 26452626
DOI: 10.1002/pro.2825

Experimental method

X-RAY DIFFRACTION (2.052 Å)