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TitleRestricting the ligand-linked heme movement in Scapharca dimeric hemoglobin reveals tight coupling between distal and proximal contributions to cooperativity.
Journal, issue, pagesBiochemistry, Vol. 40, Page 14795-14805, Year 2001
Publish dateSep 4, 2001 (structure data deposition date)
AuthorsKnapp, J.E. / Gibson, Q.H. / Cushing, L. / Royer Jr., W.E.
External linksBiochemistry / PubMed:11732898
MethodsX-ray diffraction
Resolution1.5 - 2.2 Å
Structure data

PDB-1jwn:
Crystal Structure of Scapharca inaequivalvis HbI, I114F Mutant Ligated to Carbon Monoxide.
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-1jzk:
Crystal Structure of Scapharca inaequivalvis HbI, I114F mutant (deoxy)
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-1jzl:
Crystal structure of Sapharca inaequivalvis HbI, I114M mutant ligated to carbon monoxide.
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-1jzm:
Crystal Structure of Scapharca inaequivalvis HbI, I114M Mutant in the Absence of ligand.
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-CMO:
CARBON MONOXIDE

ChemComp-HOH:
WATER

Source
  • scapharca inaequivalvis (ark clam)
KeywordsOXYGEN STORAGE/TRANSPORT / Invertebrate Hemoglobin / Allostery / Cooperativity / Oxygen-binding Protein / Heme Protein / OXYGEN STORAGE-TRANSPORT COMPLEX / invertebrate / hemoglobin / oxygen-binding / oxygen-transport

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