1ljw
From Proteopedia
Line 1: | Line 1: | ||
- | [[Image:1ljw.gif|left|200px]]<br /> | + | [[Image:1ljw.gif|left|200px]]<br /><applet load="1ljw" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1ljw" size=" | + | |
caption="1ljw, resolution 2.16Å" /> | caption="1ljw, resolution 2.16Å" /> | ||
'''Crystal Structure of Human Carbonmonoxy Hemoglobin at 2.16 A: A Snapshot of the Allosteric Transition'''<br /> | '''Crystal Structure of Human Carbonmonoxy Hemoglobin at 2.16 A: A Snapshot of the Allosteric Transition'''<br /> | ||
==Overview== | ==Overview== | ||
- | A 2.16 A resolution structure of high-salt human carbonmonoxyhemoglobin | + | 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== | ==Disease== | ||
Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
- | 1LJW 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 PO4, CMO and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1LJW 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=PO4:'>PO4</scene>, <scene name='pdbligand=CMO:'>CMO</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJW OCA]. |
==Reference== | ==Reference== | ||
Line 17: | Line 16: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
- | [[Category: Abraham, D | + | [[Category: Abraham, D J.]] |
- | [[Category: Burnett, J | + | [[Category: Burnett, J C.]] |
- | [[Category: Musayev, F | + | [[Category: Musayev, F N.]] |
[[Category: Nokuri, S.]] | [[Category: Nokuri, S.]] | ||
- | [[Category: Safo, M | + | [[Category: Safo, M K.]] |
[[Category: CMO]] | [[Category: CMO]] | ||
[[Category: HEM]] | [[Category: HEM]] | ||
Line 30: | Line 29: | ||
[[Category: r state]] | [[Category: r state]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:35 2008'' |
Revision as of 11:45, 21 February 2008
|
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 , and 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 Thu Feb 21 13:45:35 2008
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