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3UHU

HBI (M37A) deoxy

Summary for 3UHU
Entry DOI10.2210/pdb3uhu/pdb
Related3SDH 3UGY 3UGZ 3UH3 3UH5 3UH6 3UH7 3UHB 3UHC 3UHD 3UHE 3UHG 3UHH 3UHI 3UHK 3UHN 3UHQ 3UHR 3UHS 3UHT 3UHV 3UHW 3UHX 3UHY 3UHZ 3UI0 4SDH
DescriptorGlobin-1, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
Functional Keywordsallostery, oxygen binding, oxygen storage, oxygen transport
Biological sourceScapharca inaequivalvis (Ark clam)
Cellular locationCytoplasm: P02213
Total number of polymer chains2
Total formula weight33047.34
Authors
Ren, Z.,Srajer, V.,Knapp, J.E.,Royer Jr., W.E. (deposition date: 2011-11-03, release date: 2011-12-28, Last modification date: 2023-09-13)
Primary citationRen, Z.,Srajer, V.,Knapp, J.E.,Royer, W.E.
Cooperative macromolecular device revealed by meta-analysis of static and time-resolved structures.
Proc.Natl.Acad.Sci.USA, 109:107-112, 2012
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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