1qfh | pdb_00001qfh
DIMERIZATION OF GELATION FACTOR FROM DICTYOSTELIUM DISCOIDEUM: CRYSTAL STRUCTURE OF ROD DOMAINS 5 AND 6
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Overview
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.
About this Structure
1QFH is a Single protein structure of sequence from Dictyostelium discoideum. Full crystallographic information is available from OCA.
Reference
Structural basis for dimerization of the Dictyostelium gelation factor (ABP120) rod., McCoy AJ, Fucini P, Noegel AA, Stewart M, Nat Struct Biol. 1999 Sep;6(9):836-41. PMID:10467095
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