The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms

J R H Tame; J C Wilson; R E Weber

The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms

J R H Tame, J C Wilson, R E Weber

Research output: Contribution to journal › Article › peer-review

Abstract

We have determined the X-ray crystallographic structure of trout Hb I in both the deoxy and carbonmonoxy forms to resolution limits of 2.3 Angstrom and 2.5 Angstrom, respectively. The overall fold of the molecule is highly similar to that of human HbA despite the low level of sequence identity between these proteins. Trout Hb I is unusual in displaying almost no pH dependence of oxygen binding affinity, and (at most) very weak interactions with heterotropic effector ligands such as organic phosphates. Comparison of the two quaternary states of the protein indicates how such effects are minimised and how the low-affinity T state of the protein is stabilised in the absence of heterotropic interactions. (C) 1996 Academic Press Limited

Original language	English
Pages (from-to)	749-760
Number of pages	12
Journal	Journal of Molecular Biology
Volume	259
Issue number	4
Publication status	Published - 21 Jun 1996

Keywords

crystallography
haemoglobin
Bohr effect
AMINO-ACID-SEQUENCE
X-RAY-DIFFRACTION
HUMAN-HEMOGLOBIN
LIGAND-BINDING
HUMAN DEOXYHEMOGLOBIN
FUNCTIONAL PROPERTIES
SALMO-IRIDEUS
STEREOCHEMISTRY
RESOLUTION
FISH

Cite this

@article{b4baa138b8214c6bbce3c830d951c823,

title = "The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms",

abstract = "We have determined the X-ray crystallographic structure of trout Hb I in both the deoxy and carbonmonoxy forms to resolution limits of 2.3 Angstrom and 2.5 Angstrom, respectively. The overall fold of the molecule is highly similar to that of human HbA despite the low level of sequence identity between these proteins. Trout Hb I is unusual in displaying almost no pH dependence of oxygen binding affinity, and (at most) very weak interactions with heterotropic effector ligands such as organic phosphates. Comparison of the two quaternary states of the protein indicates how such effects are minimised and how the low-affinity T state of the protein is stabilised in the absence of heterotropic interactions. (C) 1996 Academic Press Limited",

keywords = "crystallography, haemoglobin, Bohr effect, AMINO-ACID-SEQUENCE, X-RAY-DIFFRACTION, HUMAN-HEMOGLOBIN, LIGAND-BINDING, HUMAN DEOXYHEMOGLOBIN, FUNCTIONAL PROPERTIES, SALMO-IRIDEUS, STEREOCHEMISTRY, RESOLUTION, FISH",

author = "Tame, {J R H} and Wilson, {J C} and Weber, {R E}",

year = "1996",

month = jun,

day = "21",

language = "English",

volume = "259",

pages = "749--760",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

number = "4",

}

TY - JOUR

T1 - The crystal structures of trout Hb I in the deoxy and carbonmonoxy forms

AU - Tame, J R H

AU - Wilson, J C

AU - Weber, R E

PY - 1996/6/21

Y1 - 1996/6/21

N2 - We have determined the X-ray crystallographic structure of trout Hb I in both the deoxy and carbonmonoxy forms to resolution limits of 2.3 Angstrom and 2.5 Angstrom, respectively. The overall fold of the molecule is highly similar to that of human HbA despite the low level of sequence identity between these proteins. Trout Hb I is unusual in displaying almost no pH dependence of oxygen binding affinity, and (at most) very weak interactions with heterotropic effector ligands such as organic phosphates. Comparison of the two quaternary states of the protein indicates how such effects are minimised and how the low-affinity T state of the protein is stabilised in the absence of heterotropic interactions. (C) 1996 Academic Press Limited

AB - We have determined the X-ray crystallographic structure of trout Hb I in both the deoxy and carbonmonoxy forms to resolution limits of 2.3 Angstrom and 2.5 Angstrom, respectively. The overall fold of the molecule is highly similar to that of human HbA despite the low level of sequence identity between these proteins. Trout Hb I is unusual in displaying almost no pH dependence of oxygen binding affinity, and (at most) very weak interactions with heterotropic effector ligands such as organic phosphates. Comparison of the two quaternary states of the protein indicates how such effects are minimised and how the low-affinity T state of the protein is stabilised in the absence of heterotropic interactions. (C) 1996 Academic Press Limited

KW - crystallography

KW - haemoglobin

KW - Bohr effect

KW - AMINO-ACID-SEQUENCE

KW - X-RAY-DIFFRACTION

KW - HUMAN-HEMOGLOBIN

KW - LIGAND-BINDING

KW - HUMAN DEOXYHEMOGLOBIN

KW - FUNCTIONAL PROPERTIES

KW - SALMO-IRIDEUS

KW - STEREOCHEMISTRY

KW - RESOLUTION

KW - FISH

M3 - Article

SN - 0022-2836

VL - 259

SP - 749

EP - 760

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 4

ER -