1sct
From Proteopedia
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|PDB= 1sct |SIZE=350|CAPTION= <scene name='initialview01'>1sct</scene>, resolution 2.0Å | |PDB= 1sct |SIZE=350|CAPTION= <scene name='initialview01'>1sct</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sct FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sct OCA], [http://www.ebi.ac.uk/pdbsum/1sct PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sct RCSB]</span> | ||
}} | }} | ||
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[[Category: Scapharca inaequivalvis]] | [[Category: Scapharca inaequivalvis]] | ||
[[Category: Junior, W E.Royer.]] | [[Category: Junior, W E.Royer.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: CMO]] | ||
| - | [[Category: HEM]] | ||
[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:40:19 2008'' |
Revision as of 20:40, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SCAPHARCA TETRAMERIC HEMOGLOBIN, CO-STATE
Overview
The crystal structure of the allosteric tetrameric hemoglobin from Scapharca inaequivalvis (HbII) has been determined in the carbonmonoxy liganded state using a combination of anomalous scattering and molecular replacement. The molecular model has been refined at 2.0 A resolution to a conventional R-factor of 0.173 and a free R-factor of 0.244. The tetramer is formed from two identical heterodimers. Each heterodimer is assembled with intersubunit contacts involving the E and F helices and heme groups in a manner that is very similar to that of the cooperative Scapharca homodimeric hemoglobin. In addition, the ordered water structure observed in these dimeric interfaces is quite similar. These structural similarities strongly suggest that the dimers within the Scapharca tetramer are cooperative. Subunits assemble into a tetramer in a distinctly non-tetrahedral arrangement, with the pseudo 2-fold axes of the heterodimer oriented at an angle of 74.5 degrees relative to the molecular 2-fold. This arrangement requires that two subunit types have distinct locations and contacts, despite the very similar tertiary structures. HbII polymerizes to higher-order assemblages in a ligand, proton and anion dependent fashion. The lattice contacts in the HbII-CO crystal suggest possible modes for this association.
About this Structure
1SCT is a Protein complex structure of sequences from Scapharca inaequivalvis. Full crystallographic information is available from OCA.
Reference
The 2.0 A crystal structure of Scapharca tetrameric hemoglobin: cooperative dimers within an allosteric tetramer., Royer WE Jr, Heard KS, Harrington DJ, Chiancone E, J Mol Biol. 1995 Oct 13;253(1):168-86. PMID:7473710
Page seeded by OCA on Sun Mar 30 23:40:19 2008
