1HYQ

MIND BACTERIAL CELL DIVISION REGULATOR FROM A. FULGIDUS

Summary for 1HYQ

• Entry DOI: 10.2210/pdb1hyq/pdb
• Descriptor: CELL DIVISION INHIBITOR (MIND-1) (2 entities in total)
• Functional Keywords: minc, ftsz, bacterial cell division, cell cycle
• Biological source: Archaeoglobus fulgidus
• Total number of polymer chains: 1
• Total formula weight: 27689.51

Authors

Cordell, S.C.,Lowe, J. (deposition date: 2001-01-21, release date: 2001-03-14, Last modification date: 2024-02-07)

Primary citation

Cordell, S.C.,Lowe, J.
Crystal structure of the bacterial cell division regulator MinD.
FEBS Lett., 492:160-165, 2001

PubMed Abstract: In bacterial cell division MinD plays a pivotal role, selecting the mid-cell over other sites. With MinC, MinD forms a non-specific inhibitor of division, that interacts with FtsZ. Specificity is provided by MinD's interaction with MinE at the mid-cell. We have solved the crystal structure of MinD-1 from Archaeoglobus fulgidus to 2.6 A by multiple anomalous dispersion. MinD is a classic nucleotide binding protein, related to nitrogenase iron proteins, which have a fold of a seven-stranded parallel beta-sheet, surrounded by alpha-helices. Although MinD, unlike the proteins it interacts with and those it is structurally related to, is a monomer, not a dimer.

PubMed: 11248256
DOI: 10.1016/S0014-5793(01)02216-5

Experimental method

X-RAY DIFFRACTION (2.6 Å)