1j3y

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[[Image:1j3y.jpg|left|200px]]<br /><applet load="1j3y" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1j3y.jpg|left|200px]]
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caption="1j3y, resolution 1.55&Aring;" />
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'''Direct observation of photolysis-induced tertiary structural changes in human hemoglobin; Crystal structure of alpha(Fe)-beta(Ni) hemoglobin (laser photolysed)'''<br />
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{{Structure
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|PDB= 1j3y |SIZE=350|CAPTION= <scene name='initialview01'>1j3y</scene>, resolution 1.55&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=CMO:CARBON+MONOXIDE'>CMO</scene>, <scene name='pdbligand=HNI:PROTOPORPHYRIN+IX+CONTAINING+NI(II)'>HNI</scene> and <scene name='pdbligand=2FU:BUT-2-ENEDIAL'>2FU</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''Direct observation of photolysis-induced tertiary structural changes in human hemoglobin; Crystal structure of alpha(Fe)-beta(Ni) hemoglobin (laser photolysed)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1J3Y 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=HEM:'>HEM</scene>, <scene name='pdbligand=CMO:'>CMO</scene>, <scene name='pdbligand=HNI:'>HNI</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=1J3Y OCA].
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1J3Y is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1J3Y OCA].
==Reference==
==Reference==
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Direct observation of photolysis-induced tertiary structural changes in hemoglobin., Adachi S, Park SY, Tame JR, Shiro Y, Shibayama N, Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):7039-44. Epub 2003 May 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12773618 12773618]
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Direct observation of photolysis-induced tertiary structural changes in hemoglobin., Adachi S, Park SY, Tame JR, Shiro Y, Shibayama N, Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):7039-44. Epub 2003 May 28. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12773618 12773618]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: rsgi]]
[[Category: rsgi]]
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[[Category: structural genomics]]
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[[Category: structural genomic]]
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[[Category: tertiary structure changes]]
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[[Category: tertiary structure change]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:58:34 2008''

Revision as of 09:58, 20 March 2008

Image:1j3y.jpg


PDB ID 1j3y

Drag the structure with the mouse to rotate
, resolution 1.55Å
Ligands: , , and
Coordinates: save as pdb, mmCIF, xml



Direct observation of photolysis-induced tertiary structural changes in human hemoglobin; Crystal structure of alpha(Fe)-beta(Ni) hemoglobin (laser photolysed)


Contents

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.

Disease

Known diseases associated with this structure: Erythremias, alpha- OMIM:[141800], Erythremias, beta- OMIM:[141900], Erythrocytosis OMIM:[141850], HPFH, deletion type OMIM:[141900], Heinz body anemia OMIM:[141850], Heinz body anemias, alpha- OMIM:[141800], Heinz body anemias, beta- OMIM:[141900], Hemoglobin H disease OMIM:[141850], Hypochromic microcytic anemia OMIM:[141850], Methemoglobinemias, alpha- OMIM:[141800], Methemoglobinemias, beta- OMIM:[141900], Sickle cell anemia OMIM:[141900], Thalassemia, alpha- OMIM:[141850], Thalassemia-beta, dominant inclusion-body OMIM:[141900], Thalassemias, alpha- OMIM:[141800], Thalassemias, beta- OMIM:[141900]

About this Structure

1J3Y is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Direct observation of photolysis-induced tertiary structural changes in hemoglobin., Adachi S, Park SY, Tame JR, Shiro Y, Shibayama N, Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):7039-44. Epub 2003 May 28. PMID:12773618

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