1s69
From Proteopedia
(New page: 200px<br /> <applet load="1s69" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s69, resolution 1.68Å" /> '''The X-ray structure...) |
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caption="1s69, resolution 1.68Å" /> | caption="1s69, resolution 1.68Å" /> | ||
'''The X-ray structure of the cyanobacteria Synechocystis hemoglobin "cyanoglobin" with cyanide ligand'''<br /> | '''The X-ray structure of the cyanobacteria Synechocystis hemoglobin "cyanoglobin" with cyanide ligand'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1S69 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with FLC, CYN and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1S69 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp. Synechocystis sp.] with <scene name='pdbligand=FLC:'>FLC</scene>, <scene name='pdbligand=CYN:'>CYN</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=1S69 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: truncated]] | [[Category: truncated]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:52:31 2008'' |
Revision as of 14:52, 15 February 2008
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The X-ray structure of the cyanobacteria Synechocystis hemoglobin "cyanoglobin" with cyanide ligand
Overview
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.
About this Structure
1S69 is a Single protein structure of sequence from Synechocystis sp. with , and as ligands. Full crystallographic information is available from OCA.
Reference
Crystallographic analysis of synechocystis cyanoglobin reveals the structural changes accompanying ligand binding in a hexacoordinate hemoglobin., Trent JT 3rd, Kundu S, Hoy JA, Hargrove MS, J Mol Biol. 2004 Aug 20;341(4):1097-108. PMID:15289104
Page seeded by OCA on Fri Feb 15 16:52:31 2008
Categories: Single protein | Synechocystis sp. | Hargrove, M.S. | Hoy, J.A. | III, J.T.Trent. | Kundu, S. | CYN | FLC | HEM | 2 on 2 helical fold | Cyanobacteria | Globin | Heme | Hemoglobin | Hexacoordinate | Iron | Oxygen binding | Truncated
