1r74: Difference between revisions

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[[Image:1r74.jpg|left|200px]]
{{Seed}}
[[Image:1r74.png|left|200px]]


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{{STRUCTURE_1r74|  PDB=1r74  |  SCENE=  }}  
{{STRUCTURE_1r74|  PDB=1r74  |  SCENE=  }}  


'''Crystal Structure of Human Glycine N-Methyltransferase'''
===Crystal Structure of Human Glycine N-Methyltransferase===




==Overview==
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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.
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{{ABSTRACT_PUBMED_15340920}}


==Disease==
==Disease==
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[[Category: Glycine n-methyltransferase]]
[[Category: Glycine n-methyltransferase]]
[[Category: Human]]
[[Category: Human]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 09:06:34 2008''

Revision as of 06:06, 29 July 2008

File:1r74.png

Template:STRUCTURE 1r74

Crystal Structure of Human Glycine N-Methyltransferase

Template:ABSTRACT PUBMED 15340920

Disease

Known disease associated with this structure: Glycine N-methyltransferase deficiency OMIM:[606628]

About this Structure

1R74 is a Single protein structure of sequence from Homo sapiens. 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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