1nwn
From Proteopedia
(New page: 200px<br /> <applet load="1nwn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nwn, resolution 2.80Å" /> '''Crystals of CO-HbI ...) |
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| - | [[Image:1nwn.gif|left|200px]]<br /> | + | [[Image:1nwn.gif|left|200px]]<br /><applet load="1nwn" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1nwn" size=" | + | |
caption="1nwn, resolution 2.80Å" /> | caption="1nwn, resolution 2.80Å" /> | ||
'''Crystals of CO-HbI in which the structure was converted to its unligated state, and then converted back to its original CO-ligated state.'''<br /> | '''Crystals of CO-HbI in which the structure was converted to its unligated state, and then converted back to its original CO-ligated state.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cooperative ligand binding in the dimeric hemoglobin (HbI) from the blood | + | Cooperative ligand binding in the dimeric hemoglobin (HbI) from the blood clam Scapharca inaequivalvis is mediated primarily by tertiary structural changes, but with a small quaternary rearrangement (approximately 3 degrees), based on analysis of distinct crystal forms for ligated and unligated molecules. We report here ligand transition structures in both crystal forms. Binding CO to unligated HbI crystals results in a structure that approaches, but does not attain, the full allosteric transition. In contrast, removing CO from the HbI-CO crystals results in a structure that possesses all the key low affinity attributes previously identified from analysis of HbI crystals grown in the unligated state. Subsequent binding of CO shows the reversibility of this process. The observed structural changes include the quaternary rearrangement even under the constraints of lattice interactions, demonstrating that subunit rotation is an integral component of the ligand-linked structural transition in HbI. Analysis of both crystal forms, along with data from HbI mutants, suggests that the quaternary structural change is linked to the movement of the heme group, supporting a hypothesis that the heme movement is the central event that triggers cooperative ligand binding in this hemoglobin dimer. These results show both the effects of a crystal lattice in limiting quaternary structural transitions and provide the first example of complete allosteric transitions within another crystal lattice. |
==About this Structure== | ==About this Structure== | ||
| - | 1NWN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Scapharca_inaequivalvis Scapharca inaequivalvis] with HEM and CMO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1NWN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Scapharca_inaequivalvis Scapharca inaequivalvis] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=CMO:'>CMO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NWN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Scapharca inaequivalvis]] | [[Category: Scapharca inaequivalvis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: JR., W | + | [[Category: JR., W E.Royer.]] |
| - | [[Category: Knapp, J | + | [[Category: Knapp, J E.]] |
[[Category: CMO]] | [[Category: CMO]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
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[[Category: oxygen-binding]] | [[Category: oxygen-binding]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:52 2008'' |
Revision as of 12:10, 21 February 2008
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Crystals of CO-HbI in which the structure was converted to its unligated state, and then converted back to its original CO-ligated state.
Overview
Cooperative ligand binding in the dimeric hemoglobin (HbI) from the blood clam Scapharca inaequivalvis is mediated primarily by tertiary structural changes, but with a small quaternary rearrangement (approximately 3 degrees), based on analysis of distinct crystal forms for ligated and unligated molecules. We report here ligand transition structures in both crystal forms. Binding CO to unligated HbI crystals results in a structure that approaches, but does not attain, the full allosteric transition. In contrast, removing CO from the HbI-CO crystals results in a structure that possesses all the key low affinity attributes previously identified from analysis of HbI crystals grown in the unligated state. Subsequent binding of CO shows the reversibility of this process. The observed structural changes include the quaternary rearrangement even under the constraints of lattice interactions, demonstrating that subunit rotation is an integral component of the ligand-linked structural transition in HbI. Analysis of both crystal forms, along with data from HbI mutants, suggests that the quaternary structural change is linked to the movement of the heme group, supporting a hypothesis that the heme movement is the central event that triggers cooperative ligand binding in this hemoglobin dimer. These results show both the effects of a crystal lattice in limiting quaternary structural transitions and provide the first example of complete allosteric transitions within another crystal lattice.
About this Structure
1NWN is a Single protein structure of sequence from Scapharca inaequivalvis with and as ligands. Full crystallographic information is available from OCA.
Reference
Ligand-linked structural transitions in crystals of a cooperative dimeric hemoglobin., Knapp JE, Royer WE Jr, Biochemistry. 2003 Apr 29;42(16):4640-7. PMID:12705827
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