1v4w
From Proteopedia
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| - | [[Image:1v4w.jpg|left|200px]] | + | [[Image:1v4w.jpg|left|200px]] |
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| - | '''Crystal structure of bluefin tuna hemoglobin deoxy form at pH7.5''' | + | {{Structure |
| + | |PDB= 1v4w |SIZE=350|CAPTION= <scene name='initialview01'>1v4w</scene>, resolution 1.70Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal structure of bluefin tuna hemoglobin deoxy form at pH7.5''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1V4W is a [ | + | 1V4W is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thunnus_thynnus Thunnus thynnus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V4W OCA]. |
==Reference== | ==Reference== | ||
| - | Novel mechanisms of pH sensitivity in tuna hemoglobin: a structural explanation of the root effect., Yokoyama T, Chong KT, Miyazaki G, Morimoto H, Shih DT, Unzai S, Tame JR, Park SY, J Biol Chem. 2004 Jul 2;279(27):28632-40. Epub 2004 Apr 26. PMID:[http:// | + | Novel mechanisms of pH sensitivity in tuna hemoglobin: a structural explanation of the root effect., Yokoyama T, Chong KT, Miyazaki G, Morimoto H, Shih DT, Unzai S, Tame JR, Park SY, J Biol Chem. 2004 Jul 2;279(27):28632-40. Epub 2004 Apr 26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15117955 15117955] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Thunnus thynnus]] | [[Category: Thunnus thynnus]] | ||
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[[Category: swim bladder]] | [[Category: swim bladder]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:40:52 2008'' |
Revision as of 12:40, 20 March 2008
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| , resolution 1.70Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of bluefin tuna hemoglobin deoxy form at pH7.5
Overview
The crystal structure of hemoglobin has been known for several decades, yet various features of the molecule remain unexplained or controversial. Several animal hemoglobins have properties that cannot be readily explained in terms of their amino acid sequence and known atomic models of hemoglobin. Among these, fish hemoglobins are well known for their widely varying interactions with heterotropic effector molecules and pH sensitivity. Some fish hemoglobins are almost completely insensitive to pH (within physiological limits), whereas others show extremely low oxygen affinity under acid conditions, a phenomenon called the Root effect. X-ray crystal structures of Root effect hemoglobins have not, to date, provided convincing explanations of this effect. Sequence alignments have signally failed to pinpoint the residues involved, and site-directed mutagenesis has not yielded a human hemoglobin variant with this property. We have solved the crystal structure of tuna hemoglobin in the deoxy form at low and moderate pH and in the presence of carbon monoxide at high pH. A comparison of these models shows clear evidence for novel mechanisms of pH-dependent control of ligand affinity.
About this Structure
1V4W is a Protein complex structure of sequences from Thunnus thynnus. Full crystallographic information is available from OCA.
Reference
Novel mechanisms of pH sensitivity in tuna hemoglobin: a structural explanation of the root effect., Yokoyama T, Chong KT, Miyazaki G, Morimoto H, Shih DT, Unzai S, Tame JR, Park SY, J Biol Chem. 2004 Jul 2;279(27):28632-40. Epub 2004 Apr 26. PMID:15117955
Page seeded by OCA on Thu Mar 20 14:40:52 2008
