5mba

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(New page: 200px<br /><applet load="5mba" size="450" color="white" frame="true" align="right" spinBox="true" caption="5mba, resolution 1.9&Aring;" /> '''BINDING MODE OF AZIDE...)
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'''BINDING MODE OF AZIDE TO FERRIC APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.9 ANGSTROMS RESOLUTION'''<br />
'''BINDING MODE OF AZIDE TO FERRIC APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.9 ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
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The binding mode of azide to the ferric form of Aplysia limacina myoglobin, has been studied by X-ray crystallography. The three-dimensional structure, of the complex has been refined at 1.9 A resolution to a crystallographic, R-factor of 13.9%, including 126 ordered solvent molecules. Azide binds to, the heme iron, at the sixth co-ordination position, and is oriented, towards the outer part of the distal site crevice. This orientation is, stabilized by an ionic interaction with the side-chain of Arg66 (E10), which, from an outer orientation in the 'aquo-met' ligand-free myoglobin, folds back towards the distal site in the presence of the anionic ligand., In the absence of a hydrogen bond donor residue at the distal E7 position, in Aplysia limacina myoglobin, a different polar residue, Arg66 at the E10, topological position, has been selected by molecular evolution in order to, grant ligand stabilization.
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The binding mode of azide to the ferric form of Aplysia limacina myoglobin has been studied by X-ray crystallography. The three-dimensional structure of the complex has been refined at 1.9 A resolution to a crystallographic R-factor of 13.9%, including 126 ordered solvent molecules. Azide binds to the heme iron, at the sixth co-ordination position, and is oriented towards the outer part of the distal site crevice. This orientation is stabilized by an ionic interaction with the side-chain of Arg66 (E10) which, from an outer orientation in the 'aquo-met' ligand-free myoglobin, folds back towards the distal site in the presence of the anionic ligand. In the absence of a hydrogen bond donor residue at the distal E7 position in Aplysia limacina myoglobin, a different polar residue, Arg66 at the E10 topological position, has been selected by molecular evolution in order to grant ligand stabilization.
==About this Structure==
==About this Structure==
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5MBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_limacina Aplysia limacina] with AZI, ACE and HEM as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 2MBA. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5MBA OCA].
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5MBA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_limacina Aplysia limacina] with <scene name='pdbligand=AZI:'>AZI</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 2MBA. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MBA OCA].
==Reference==
==Reference==
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[[Category: oxygen storage]]
[[Category: oxygen storage]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:36:20 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 19:15:30 2008''

Revision as of 17:15, 21 February 2008

Image:5mba.gif

5mba, resolution 1.9Å

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BINDING MODE OF AZIDE TO FERRIC APLYSIA LIMACINA MYOGLOBIN. CRYSTALLOGRAPHIC ANALYSIS AT 1.9 ANGSTROMS RESOLUTION

Overview

The binding mode of azide to the ferric form of Aplysia limacina myoglobin has been studied by X-ray crystallography. The three-dimensional structure of the complex has been refined at 1.9 A resolution to a crystallographic R-factor of 13.9%, including 126 ordered solvent molecules. Azide binds to the heme iron, at the sixth co-ordination position, and is oriented towards the outer part of the distal site crevice. This orientation is stabilized by an ionic interaction with the side-chain of Arg66 (E10) which, from an outer orientation in the 'aquo-met' ligand-free myoglobin, folds back towards the distal site in the presence of the anionic ligand. In the absence of a hydrogen bond donor residue at the distal E7 position in Aplysia limacina myoglobin, a different polar residue, Arg66 at the E10 topological position, has been selected by molecular evolution in order to grant ligand stabilization.

About this Structure

5MBA is a Single protein structure of sequence from Aplysia limacina with , and as ligands. This structure supersedes the now removed PDB entry 2MBA. Full crystallographic information is available from OCA.

Reference

Binding mode of azide to ferric Aplysia limacina myoglobin. Crystallographic analysis at 1.9 A resolution., Mattevi A, Gatti G, Coda A, Rizzi M, Ascenzi P, Brunori M, Bolognesi M, J Mol Recognit. 1991 Feb;4(1):1-6. PMID:1931125

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