1j40: Difference between revisions

No edit summary
No edit summary
Line 1: Line 1:
[[Image:1j40.gif|left|200px]]<br />
[[Image:1j40.gif|left|200px]]<br /><applet load="1j40" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1j40" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1j40, resolution 1.45&Aring;" />
caption="1j40, resolution 1.45&Aring;" />
'''Direct observation of photolysis-induced tertiary structural changes in human haemoglobin; Crystal structure of alpha(Ni)-beta(Fe-CO) hemoglobin (laser unphotolysed)'''<br />
'''Direct observation of photolysis-induced tertiary structural changes in human haemoglobin; Crystal structure of alpha(Ni)-beta(Fe-CO) hemoglobin (laser unphotolysed)'''<br />


==Overview==
==Overview==
Human Hb, an alpha2beta2 tetrameric oxygen transport protein that switches, from a T (tense) to an R (relaxed) quaternary structure during, oxygenation, has long served as a model for studying protein allostery in, general. Time-resolved spectroscopic measurements after photodissociation, of CO-liganded Hb have played a central role in exploring both protein, dynamical responses and molecular cooperativity, but the direct, visualization and the structural consequences of photodeligation have not, yet been reported. Here we present an x-ray study of structural changes, induced by photodissociation of half-liganded T-state and fully liganded, R-state human Hb at cryogenic temperatures (25-35 K). On photodissociation, of CO, structural changes involving the heme and the F-helix are more, marked in the alpha subunit than in the beta subunit, and more subtle in, the R state than in the T state. Photodeligation causes a significant, sliding motion of the T-state beta heme. Our results establish that the, structural basis of the low affinity of the T state is radically different, between the subunits, because of differences in the packing and chemical, tension at the hemes.
Human Hb, an alpha2beta2 tetrameric oxygen transport protein that switches from a T (tense) to an R (relaxed) quaternary structure during oxygenation, has long served as a model for studying protein allostery in general. Time-resolved spectroscopic measurements after photodissociation of CO-liganded Hb have played a central role in exploring both protein dynamical responses and molecular cooperativity, but the direct visualization and the structural consequences of photodeligation have not yet been reported. Here we present an x-ray study of structural changes induced by photodissociation of half-liganded T-state and fully liganded R-state human Hb at cryogenic temperatures (25-35 K). On photodissociation of CO, structural changes involving the heme and the F-helix are more marked in the alpha subunit than in the beta subunit, and more subtle in the R state than in the T state. Photodeligation causes a significant sliding motion of the T-state beta heme. Our results establish that the structural basis of the low affinity of the T state is radically different between the subunits, because of differences in the packing and chemical tension at the hemes.


==Disease==
==Disease==
Line 11: Line 10:


==About this Structure==
==About this Structure==
1J40 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HNI, HEM, CMO and 2FU as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J40 OCA].  
1J40 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HNI:'>HNI</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=CMO:'>CMO</scene> and <scene name='pdbligand=2FU:'>2FU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J40 OCA].  


==Reference==
==Reference==
Line 18: Line 17:
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Adachi, S.]]
[[Category: Adachi, S.]]
[[Category: Park, S.Y.]]
[[Category: Park, S Y.]]
[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Shibayama, N.]]
[[Category: Shibayama, N.]]
[[Category: Shiro, Y.]]
[[Category: Shiro, Y.]]
[[Category: Tame, J.R.H.]]
[[Category: Tame, J R.H.]]
[[Category: 2FU]]
[[Category: 2FU]]
[[Category: CMO]]
[[Category: CMO]]
Line 33: Line 32:
[[Category: tertiary structure changes]]
[[Category: tertiary structure changes]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:37:01 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:42 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA