This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1bhj
From Proteopedia
(New page: 200px<br /><applet load="1bhj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bhj, resolution 2.5Å" /> '''CRYSTAL STRUCTURE OF ...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1bhj.gif|left|200px]]<br /><applet load="1bhj" size=" | + | [[Image:1bhj.gif|left|200px]]<br /><applet load="1bhj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1bhj, resolution 2.5Å" /> | caption="1bhj, resolution 2.5Å" /> | ||
'''CRYSTAL STRUCTURE OF APO-GLYCINE N-METHYLTRANSFERASE (GNMT)'''<br /> | '''CRYSTAL STRUCTURE OF APO-GLYCINE N-METHYLTRANSFERASE (GNMT)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the recombinant apo-form of glycine | + | The crystal structure of the recombinant apo-form of glycine N-methyltransferase (GNMT) has been determined at 2.5 A resolution. GNMT is a tetrameric enzyme (monomer Mr = 32,423Da, 292 amino acids) that catalyzes the transfer of a methyl group from S-adenosylmethionine (AdoMet) to glycine with the formation of S-adenosylhomocysteine (AdoHcy) and sarcosine (N-methylglycine). GNMT is a regulatory enzyme, which is inhibited by 5-methyltetrahydrofolate pentaglutamate and believed to control the ratio of AdoMet to AdoHcy in tissues. The crystals belong to the orthorhombic space group P2(1)2(1)2 (a = 85.39, b = 174.21, c = 44.71 A) and contain one dimer per asymmetric unit. The AdoMet-GNMT structure served as the starting model. The structure was refined to an R-factor of 21.9%. Each monomer is a three-domain structure with a large cavity enclosed by the three domains. The tetramer resembles a square with a central channel about which N-terminal domains are intertwined. Only localized changes of the residues involved in the binding pocket are observed for the apo-GNMT structure when compared to that determined in the presence of substrate and substrate analog. |
==About this Structure== | ==About this Structure== | ||
| - | 1BHJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Glycine_N-methyltransferase Glycine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.20 2.1.1.20] Full crystallographic information is available from [http:// | + | 1BHJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Active as [http://en.wikipedia.org/wiki/Glycine_N-methyltransferase Glycine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.20 2.1.1.20] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHJ OCA]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Newcomer, M | + | [[Category: Newcomer, M E.]] |
[[Category: Pattanayek, R.]] | [[Category: Pattanayek, R.]] | ||
[[Category: Wagner, C.]] | [[Category: Wagner, C.]] | ||
| Line 20: | Line 20: | ||
[[Category: methyltransferase]] | [[Category: methyltransferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:55:21 2008'' |
Revision as of 09:55, 21 February 2008
|
CRYSTAL STRUCTURE OF APO-GLYCINE N-METHYLTRANSFERASE (GNMT)
Overview
The crystal structure of the recombinant apo-form of glycine N-methyltransferase (GNMT) has been determined at 2.5 A resolution. GNMT is a tetrameric enzyme (monomer Mr = 32,423Da, 292 amino acids) that catalyzes the transfer of a methyl group from S-adenosylmethionine (AdoMet) to glycine with the formation of S-adenosylhomocysteine (AdoHcy) and sarcosine (N-methylglycine). GNMT is a regulatory enzyme, which is inhibited by 5-methyltetrahydrofolate pentaglutamate and believed to control the ratio of AdoMet to AdoHcy in tissues. The crystals belong to the orthorhombic space group P2(1)2(1)2 (a = 85.39, b = 174.21, c = 44.71 A) and contain one dimer per asymmetric unit. The AdoMet-GNMT structure served as the starting model. The structure was refined to an R-factor of 21.9%. Each monomer is a three-domain structure with a large cavity enclosed by the three domains. The tetramer resembles a square with a central channel about which N-terminal domains are intertwined. Only localized changes of the residues involved in the binding pocket are observed for the apo-GNMT structure when compared to that determined in the presence of substrate and substrate analog.
About this Structure
1BHJ is a Single protein structure of sequence from Rattus norvegicus. Active as Glycine N-methyltransferase, with EC number 2.1.1.20 Full crystallographic information is available from OCA.
Reference
Crystal structure of apo-glycine N-methyltransferase (GNMT)., Pattanayek R, Newcomer ME, Wagner C, Protein Sci. 1998 Jun;7(6):1326-31. PMID:9655336
Page seeded by OCA on Thu Feb 21 11:55:21 2008
