1dm1
From Proteopedia
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| - | [[Image:1dm1.jpg|left|200px]] | + | [[Image:1dm1.jpg|left|200px]] |
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| - | '''2.0 A CRYSTAL STRUCTURE OF THE DOUBLE MUTANT H(E7)V, T(E10)R OF MYOGLOBIN FROM APLYSIA LIMACINA''' | + | {{Structure |
| + | |PDB= 1dm1 |SIZE=350|CAPTION= <scene name='initialview01'>1dm1</scene>, resolution 1.99Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=HEM:PROTOPORPHYRIN IX CONTAINING FE'>HEM</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''2.0 A CRYSTAL STRUCTURE OF THE DOUBLE MUTANT H(E7)V, T(E10)R OF MYOGLOBIN FROM APLYSIA LIMACINA''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DM1 is a [ | + | 1DM1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aplysia_limacina Aplysia limacina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DM1 OCA]. |
==Reference== | ==Reference== | ||
| - | Engineering His(E7) affects the control of heme reactivity in Aplysia limacina myoglobin., Federici L, Savino C, Musto R, Travaglini-Allocatelli C, Cutruzzola F, Brunori M, Biochem Biophys Res Commun. 2000 Mar 5;269(1):58-63. PMID:[http:// | + | Engineering His(E7) affects the control of heme reactivity in Aplysia limacina myoglobin., Federici L, Savino C, Musto R, Travaglini-Allocatelli C, Cutruzzola F, Brunori M, Biochem Biophys Res Commun. 2000 Mar 5;269(1):58-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10694477 10694477] |
[[Category: Aplysia limacina]] | [[Category: Aplysia limacina]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: globin fold]] | [[Category: globin fold]] | ||
| - | ''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 10:40:37 2008'' |
Revision as of 08:40, 20 March 2008
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| , resolution 1.99Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
2.0 A CRYSTAL STRUCTURE OF THE DOUBLE MUTANT H(E7)V, T(E10)R OF MYOGLOBIN FROM APLYSIA LIMACINA
Overview
Aplysia limacina myoglobin lacks the distal histidine (His (E7)) and displays a ligand stabilization mechanism based on Arg(E10). The double mutant Val(E7)His-Arg(E10)Thr has been prepared to engineer the role of His(E7), typical of mammalian myoglobins, in a different globin framework. The 2.0 A crystal structure of Val(E7)His-Arg(E10)Thr met-Mb mutant reveals that the His(E7) side chain points out of the distal pocket, providing an explanation for the observed failure to stabilize the Fe(II) bound oxygen in the ferrous myoglobin. Moreover, spectroscopic analysis together with kinetic data on azide binding to met-myoglobin are reported and discussed in terms of the presence of a water molecule at coordination distance from the heme iron.
About this Structure
1DM1 is a Single protein structure of sequence from Aplysia limacina. Full crystallographic information is available from OCA.
Reference
Engineering His(E7) affects the control of heme reactivity in Aplysia limacina myoglobin., Federici L, Savino C, Musto R, Travaglini-Allocatelli C, Cutruzzola F, Brunori M, Biochem Biophys Res Commun. 2000 Mar 5;269(1):58-63. PMID:10694477
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