1a4f

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(New page: 200px<br /> <applet load="1a4f" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a4f, resolution 2.0&Aring;" /> '''BAR-HEADED GOOSE HEM...)
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'''BAR-HEADED GOOSE HEMOGLOBIN (OXY FORM)'''<br />
'''BAR-HEADED GOOSE HEMOGLOBIN (OXY FORM)'''<br />
==Overview==
==Overview==
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We have determined the crystal structure of bar-headed goose haemoglobin, in the oxy form to a resolution of 2.0 A. The R-factor of the model is, 19.8%. The structure is similar to human HbA, but contacts between the, subunits show slightly altered packing of the tetramer. Bar-headed goose, blood shows a greatly elevated oxygen affinity compared to closely related, species of geese. This is apparently due to a single proline to alanine, mutation at the alpha 1 beta 1 interface which destabilises the T state of, the protein. The beta chain N and C termini are well-localized, and, together with other neighbouring basic groups they form a strongly, positively charged groove at the entrance to the central cavity around the, molecular dyad. The well-ordered conformation and the three-dimensional, distribution of positive charges clearly indicate this area to be the, inositol pentaphosphate binding site of bird haemoglobins.
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We have determined the crystal structure of bar-headed goose haemoglobin in the oxy form to a resolution of 2.0 A. The R-factor of the model is 19.8%. The structure is similar to human HbA, but contacts between the subunits show slightly altered packing of the tetramer. Bar-headed goose blood shows a greatly elevated oxygen affinity compared to closely related species of geese. This is apparently due to a single proline to alanine mutation at the alpha 1 beta 1 interface which destabilises the T state of the protein. The beta chain N and C termini are well-localized, and together with other neighbouring basic groups they form a strongly positively charged groove at the entrance to the central cavity around the molecular dyad. The well-ordered conformation and the three-dimensional distribution of positive charges clearly indicate this area to be the inositol pentaphosphate binding site of bird haemoglobins.
==About this Structure==
==About this Structure==
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1A4F is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Anser_indicus Anser indicus] with HEM and OXY as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1A4F OCA].
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1A4F is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Anser_indicus Anser indicus] with <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=OXY:'>OXY</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4F OCA].
==Reference==
==Reference==
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[[Category: respiratory protein]]
[[Category: respiratory protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 12:56:26 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:40:43 2008''

Revision as of 09:40, 21 February 2008

Image:1a4f.gif

1a4f, resolution 2.0Å

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BAR-HEADED GOOSE HEMOGLOBIN (OXY FORM)

Overview

We have determined the crystal structure of bar-headed goose haemoglobin in the oxy form to a resolution of 2.0 A. The R-factor of the model is 19.8%. The structure is similar to human HbA, but contacts between the subunits show slightly altered packing of the tetramer. Bar-headed goose blood shows a greatly elevated oxygen affinity compared to closely related species of geese. This is apparently due to a single proline to alanine mutation at the alpha 1 beta 1 interface which destabilises the T state of the protein. The beta chain N and C termini are well-localized, and together with other neighbouring basic groups they form a strongly positively charged groove at the entrance to the central cavity around the molecular dyad. The well-ordered conformation and the three-dimensional distribution of positive charges clearly indicate this area to be the inositol pentaphosphate binding site of bird haemoglobins.

About this Structure

1A4F is a Protein complex structure of sequences from Anser indicus with and as ligands. Full crystallographic information is available from OCA.

Reference

The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form)., Zhang J, Hua Z, Tame JR, Lu G, Zhang R, Gu X, J Mol Biol. 1996 Jan 26;255(3):484-93. PMID:8568892

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