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| [[Image:1s6a.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1s6a| PDB=1s6a | SCENE= }} | | {{STRUCTURE_1s6a| PDB=1s6a | SCENE= }} |
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| '''The X-ray structure of the cyanobacteria Synechocystis hemoglobin "cyanoglobin" with azide ligand'''
| | ===The X-ray structure of the cyanobacteria Synechocystis hemoglobin "cyanoglobin" with azide ligand=== |
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| ==Overview==
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| The crystal structures of cyanide and azide-bound forms of the truncated hemoglobin from Synechocystis are presented at 1.8 angstroms resolution. A comparison with the structure of the endogenously liganded protein reveals a conformational shift unprecedented in hemoglobins, and provides the first picture of a hexacoordinate hemoglobin in both the bis-histidyl and the exogenously coordinated states. The structural changes between the different conformations are confined to two regions of the protein; the B helix, and the E helix, including the EF loop. A molecular "hinge" controlling movement of the E helix is observed in the EF loop, which is composed of three principal structural elements: Arg64, the heme-d-propionate, and a three-residue extension of the F helix. Additional features of the structural transition between the two protein conformations are discussed as they relate to the complex ligand-binding behavior observed in hexacoordinate hemoglobins, and the potential physiological function of this class of proteins. | | The line below this paragraph, {{ABSTRACT_PUBMED_15289104}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15289104 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15289104}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Oxygen binding]] | | [[Category: Oxygen binding]] |
| [[Category: Truncated]] | | [[Category: Truncated]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:21:18 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:36:04 2008'' |
