3QOB

Mechanical Coupling Controls Cooperative Ligand Binding in a Homodimeric Hemoglobin

3QOB の概要

• エントリーDOI: 10.2210/pdb3qob/pdb
• 分子名称: Globin-1, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE (3 entities in total)
• 機能のキーワード: time-resolved, laue diffraction, dynamic crystallography, heterogeneous structure, oxygen transport
• 由来する生物種: Anadara inaequivalvis (Inequivalve ark)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33221.63

構造登録者

Ren, Z. (登録日: 2011-02-09, 公開日: 2020-06-03, 最終更新日: 2023-09-20)

主引用文献

Ren, Z.,Srajer, V.,Knapp, J.E.,Royer Jr., W.E.
Cooperative macromolecular device revealed by meta-analysis of static and time-resolved structures.
Proc.Natl.Acad.Sci.USA, 109:107-112, 2012

PubMed Abstract: Here we present a meta-analysis of a large collection of static structures of a protein in the Protein Data Bank in order to extract the progression of structural events during protein function. We apply this strategy to the homodimeric hemoglobin HbI from Scapharca inaequivalvis. We derive a simple dynamic model describing how binding of the first ligand in one of the two chemically identical subunits facilitates a second binding event in the other partner subunit. The results of our ultrafast time-resolved crystallographic studies support this model. We demonstrate that HbI functions like a homodimeric mechanical device, such as pliers or scissors. Ligand-induced motion originating in one subunit is transmitted to the other via conserved pivot points, where the E and F' helices from two partner subunits are "bolted" together to form a stable dimer interface permitting slight relative rotation but preventing sliding.

PubMed: 22171006
DOI: 10.1073/pnas.1109213108

実験手法

X-RAY DIFFRACTION (1.6 Å)