We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1nbh

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nbh.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1nbh.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nbh| PDB=1nbh | SCENE= }}
{{STRUCTURE_1nbh| PDB=1nbh | SCENE= }}
-
'''Structure of glycine N-methyltransferase complexed with S-adenosylmethionine and acetate, GNMT:SAM:Ace'''
+
===Structure of glycine N-methyltransferase complexed with S-adenosylmethionine and acetate, GNMT:SAM:Ace===
-
==Overview==
+
<!--
-
Methyltransfer reactions are some of the most important reactions in biological systems. Glycine N-methyltransferase (GNMT) catalyzes the S-adenosyl-l-methionine- (SAM-) dependent methylation of glycine to form sarcosine. Unlike most SAM-dependent methyltransferases, GNMT has a relatively high value and is weakly inhibited by the product S-adenosyl-l-homocysteine (SAH). The major role of GNMT is believed to be the regulation of the cellular SAM/SAH ratio, which is thought to play a key role in SAM-dependent methyltransfer reactions. Crystal structures of GNMT complexed with SAM and acetate (a potent competitive inhibitor of Gly) and the R175K mutated enzyme complexed with SAM were determined at 2.8 and 3.0 A resolutions, respectively. With these crystal structures and the previously determined structures of substrate-free enzyme, a catalytic mechanism has been proposed. Structural changes occur in the transitions from the substrate-free to the binary complex and from the binary to the ternary complex. In the ternary complex stage, an alpha-helix in the N-terminus undergoes a major conformational change. As a result, the bound SAM is firmly connected to protein and a "Gly pocket" is created near the bound SAM. The second substrate Gly binds to Arg175 and is brought into the Gly pocket. Five hydrogen bonds connect the Gly in the proximity of the bound SAM and orient the lone pair orbital on the amino nitrogen (N) of Gly toward the donor methyl group (C(E)) of SAM. Thermal motion of the enzyme leads to a collision of the N and C(E) so that a S(N)2 methyltransfer reaction occurs. The proposed mechanism is supported by mutagenesis studies.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12859184}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12859184 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12859184}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Methyltransferase]]
[[Category: Methyltransferase]]
[[Category: S-adenosylmethionine]]
[[Category: S-adenosylmethionine]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:19:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 16:08:33 2008''

Revision as of 13:08, 29 July 2008

Image:1nbh.png

Template:STRUCTURE 1nbh

Structure of glycine N-methyltransferase complexed with S-adenosylmethionine and acetate, GNMT:SAM:Ace

Template:ABSTRACT PUBMED 12859184

About this Structure

1NBH is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Catalytic mechanism of glycine N-methyltransferase., Takata Y, Huang Y, Komoto J, Yamada T, Konishi K, Ogawa H, Gomi T, Fujioka M, Takusagawa F, Biochemistry. 2003 Jul 22;42(28):8394-402. PMID:12859184

Page seeded by OCA on Tue Jul 29 16:08:33 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nbh"
Personal tools