1r8y
From Proteopedia
(New page: 200px<br /><applet load="1r8y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r8y, resolution 3.00Å" /> '''Crystal Structure of...) |
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| - | [[Image:1r8y.gif|left|200px]]<br /><applet load="1r8y" size=" | + | [[Image:1r8y.gif|left|200px]]<br /><applet load="1r8y" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r8y, resolution 3.00Å" /> | caption="1r8y, resolution 3.00Å" /> | ||
'''Crystal Structure of Mouse Glycine N-Methyltransferase (Monoclinic Form)'''<br /> | '''Crystal Structure of Mouse Glycine N-Methyltransferase (Monoclinic Form)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Glycine N-methyltransferases (GNMTs) from three mammalian sources were | + | Glycine N-methyltransferases (GNMTs) from three mammalian sources were compared with respect to their crystal structures and kinetic parameters. The crystal structure for the rat enzyme was published previously. Human and mouse GNMT were expressed in Escherichia coli in order to determine their crystal structures. Mouse GNMT was crystallized in two crystal forms, a monoclinic form and a tetragonal form. Comparison of the three structures reveals subtle differences, which may relate to the different kinetic properties of the enzymes.The flexible character of several loops surrounding the active site, along with an analysis of the active site boundaries, indicates that the observed conformations of human and mouse GNMTs are more open than that of the rat enzyme. There is an increase in kcat when going from rat to mouse to human, suggesting a correlation with the increased flexibility of some structural elements of the respective enzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1R8Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with BME as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1R8Y is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=BME:'>BME</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R8Y OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Luka, Z.]] | [[Category: Luka, Z.]] | ||
| - | [[Category: Newcomer, M | + | [[Category: Newcomer, M E.]] |
[[Category: Pakhomova, S.]] | [[Category: Pakhomova, S.]] | ||
[[Category: Wagner, C.]] | [[Category: Wagner, C.]] | ||
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[[Category: glycine n-methyltransferase]] | [[Category: glycine n-methyltransferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:48:19 2008'' |
Revision as of 12:48, 21 February 2008
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Crystal Structure of Mouse Glycine N-Methyltransferase (Monoclinic Form)
Overview
Glycine N-methyltransferases (GNMTs) from three mammalian sources were compared with respect to their crystal structures and kinetic parameters. The crystal structure for the rat enzyme was published previously. Human and mouse GNMT were expressed in Escherichia coli in order to determine their crystal structures. Mouse GNMT was crystallized in two crystal forms, a monoclinic form and a tetragonal form. Comparison of the three structures reveals subtle differences, which may relate to the different kinetic properties of the enzymes.The flexible character of several loops surrounding the active site, along with an analysis of the active site boundaries, indicates that the observed conformations of human and mouse GNMTs are more open than that of the rat enzyme. There is an increase in kcat when going from rat to mouse to human, suggesting a correlation with the increased flexibility of some structural elements of the respective enzymes.
About this Structure
1R8Y is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes., Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME, Proteins. 2004 Nov 1;57(2):331-7. PMID:15340920
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