1QFH

DIMERIZATION OF GELATION FACTOR FROM DICTYOSTELIUM DISCOIDEUM: CRYSTAL STRUCTURE OF ROD DOMAINS 5 AND 6

Summary for 1QFH

• Entry DOI: 10.2210/pdb1qfh/pdb
• Descriptor: PROTEIN (GELATION FACTOR) (2 entities in total)
• Functional Keywords: actin binding protein, immunoglobulin, gelation factor, abp-120
• Biological source: Dictyostelium discoideum
• Total number of polymer chains: 2
• Total formula weight: 44711.19

Authors

Mccoy, A.J.,Fucini, P.,Noegel, A.A.,Stewart, M. (deposition date: 1999-04-11, release date: 1999-04-16, Last modification date: 2023-12-27)

Primary citation

McCoy, A.J.,Fucini, P.,Noegel, A.A.,Stewart, M.
Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod.
Nat.Struct.Biol., 6:836-841, 1999

PubMed Abstract: Gelation factor (ABP120) is one of the principal actin-cross-linking proteins of Dictyostelium discoideum. The extended molecule has an N-terminal 250-residue actin-binding domain and a rod constructed from six 100-residue repeats that have an Ig fold. The ability to dimerize is crucial to the actin cross-linking function of gelation factor and is mediated by the rod in which the two chains are arranged in an antiparallel fashion. We report the 2.2 A resolution crystal structure of rod domains 5 and 6, which shows that dimerization is mediated primarily by rod domain 6 and is the result of a double edge-to-edge extension of beta-sheets. Thus, contrary to earlier proposals, the chains of the dimeric gelation factor molecule overlap only within domain 6, and domains 1-5 do not pair with domains from the other chain. This information allows construction of a model of the gelation factor molecule and suggests how the chains in the related molecule filamin (ABP280) may interact.

PubMed: 10467095
DOI: 10.1038/12296

Experimental method

X-RAY DIFFRACTION (2.2 Å)