1ljw
From Proteopedia
(New page: 200px<br /> <applet load="1ljw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ljw, resolution 2.16Å" /> '''Crystal Structure o...) |
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==Overview== | ==Overview== | ||
A 2.16 A resolution structure of high-salt human carbonmonoxyhemoglobin, crystallized at pH 6.4 is reported. The quaternary structure is similar to, that of 'classic' R-state hemoglobin; however, subtle but significant, tertiary structural changes are observed at the alpha(1)beta(2) and, symmetrically equivalent alpha(2)beta(1) interfaces--these are the key, subunit interfaces that govern the allosteric transition between the R and, T states. Specifically, the movement and weakening of two important, hydrogen bonds that are diagnostic for R-state structures, beta(2)His97-alpha(1)Thr38 and beta(2)Arg40-alpha(1)Thr41, have been, observed. In addition, a phosphate molecule bound between the two, beta-subunits (at the entrance to the central water cavity) has been, identified and electron density indicates that this molecule occupies two, alternate positions that are related by the dyad axis. Both positions, superimpose on the 2,3-diphosphoglycerate binding site. One phosphate, conformer interacts with beta(2)Asn139, beta(1)His143 and beta(1)His146, while the second interacts with symmetry-related counterparts, (beta(1)Asn139, beta(2)His143 and beta(2)His146). | A 2.16 A resolution structure of high-salt human carbonmonoxyhemoglobin, crystallized at pH 6.4 is reported. The quaternary structure is similar to, that of 'classic' R-state hemoglobin; however, subtle but significant, tertiary structural changes are observed at the alpha(1)beta(2) and, symmetrically equivalent alpha(2)beta(1) interfaces--these are the key, subunit interfaces that govern the allosteric transition between the R and, T states. Specifically, the movement and weakening of two important, hydrogen bonds that are diagnostic for R-state structures, beta(2)His97-alpha(1)Thr38 and beta(2)Arg40-alpha(1)Thr41, have been, observed. In addition, a phosphate molecule bound between the two, beta-subunits (at the entrance to the central water cavity) has been, identified and electron density indicates that this molecule occupies two, alternate positions that are related by the dyad axis. Both positions, superimpose on the 2,3-diphosphoglycerate binding site. One phosphate, conformer interacts with beta(2)Asn139, beta(1)His143 and beta(1)His146, while the second interacts with symmetry-related counterparts, (beta(1)Asn139, beta(2)His143 and beta(2)His146). | ||
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+ | ==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== | ||
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[[Category: r state]] | [[Category: r state]] | ||
- | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:02:05 2007'' |
Revision as of 15:55, 12 November 2007
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Crystal Structure of Human Carbonmonoxy Hemoglobin at 2.16 A: A Snapshot of the Allosteric Transition
Contents |
Overview
A 2.16 A resolution structure of high-salt human carbonmonoxyhemoglobin, crystallized at pH 6.4 is reported. The quaternary structure is similar to, that of 'classic' R-state hemoglobin; however, subtle but significant, tertiary structural changes are observed at the alpha(1)beta(2) and, symmetrically equivalent alpha(2)beta(1) interfaces--these are the key, subunit interfaces that govern the allosteric transition between the R and, T states. Specifically, the movement and weakening of two important, hydrogen bonds that are diagnostic for R-state structures, beta(2)His97-alpha(1)Thr38 and beta(2)Arg40-alpha(1)Thr41, have been, observed. In addition, a phosphate molecule bound between the two, beta-subunits (at the entrance to the central water cavity) has been, identified and electron density indicates that this molecule occupies two, alternate positions that are related by the dyad axis. Both positions, superimpose on the 2,3-diphosphoglycerate binding site. One phosphate, conformer interacts with beta(2)Asn139, beta(1)His143 and beta(1)His146, while the second interacts with symmetry-related counterparts, (beta(1)Asn139, beta(2)His143 and beta(2)His146).
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
1LJW is a Protein complex structure of sequences from Homo sapiens with PO4, CMO and HEM as ligands. Full crystallographic information is available from OCA.
Reference
Structure of human carbonmonoxyhemoglobin at 2.16 A: a snapshot of the allosteric transition., Safo MK, Burnett JC, Musayev FN, Nokuri S, Abraham DJ, Acta Crystallogr D Biol Crystallogr. 2002 Dec;58(Pt 12):2031-7. Epub 2002, Nov 23. PMID:12454461
Page seeded by OCA on Mon Nov 12 18:02:05 2007
Categories: Homo sapiens | Protein complex | Abraham, D.J. | Burnett, J.C. | Musayev, F.N. | Nokuri, S. | Safo, M.K. | CMO | HEM | PO4 | Allosteric | Carbonmonoxy | Hemoglobin | R state