This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1j3y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1j3y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j3y, resolution 1.55&Aring;" /> '''Direct observation ...)
Line 6: Line 6:
==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==
 +
Known diseases associated with this structure: Erythremias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Erythremias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Erythrocytosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], HPFH, deletion type OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Heinz body anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Heinz body anemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Heinz body anemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Hemoglobin H disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Hypochromic microcytic anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Methemoglobinemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Methemoglobinemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Sickle cell anemia OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Thalassemia, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141850 141850]], Thalassemia-beta, dominant inclusion-body OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]], Thalassemias, alpha- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141800 141800]], Thalassemias, beta- OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=141900 141900]]
==About this Structure==
==About this Structure==
Line 30: Line 33:
[[Category: tertiary structure changes]]
[[Category: tertiary structure changes]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 13:09:42 2007''
+
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:36:56 2007''

Revision as of 15:30, 12 November 2007


1j3y, resolution 1.55Å

Drag the structure with the mouse to rotate

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 with HEM, CMO, HNI and 2FU as ligands. 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

Page seeded by OCA on Mon Nov 12 17:36:56 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools