1v4x
From Proteopedia
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|PDB= 1v4x |SIZE=350|CAPTION= <scene name='initialview01'>1v4x</scene>, resolution 1.60Å | |PDB= 1v4x |SIZE=350|CAPTION= <scene name='initialview01'>1v4x</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1v4u|1V4U]], [[1v4w|1V4W]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v4x OCA], [http://www.ebi.ac.uk/pdbsum/1v4x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v4x RCSB]</span> | ||
}} | }} | ||
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[[Category: Unzai, S.]] | [[Category: Unzai, S.]] | ||
[[Category: Yokoyama, T.]] | [[Category: Yokoyama, T.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: HEM]] | ||
[[Category: erythrocyte]] | [[Category: erythrocyte]] | ||
[[Category: heme]] | [[Category: heme]] | ||
| Line 40: | Line 41: | ||
[[Category: swim bladder]] | [[Category: swim bladder]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:19:32 2008'' |
Revision as of 21:19, 30 March 2008
| |||||||
| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Related: | 1V4U, 1V4W
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of bluefin tuna hemoglobin deoxy form at pH5.0
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
1V4X 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 Mon Mar 31 00:19:32 2008
