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.

1nv8

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1nv8.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1nv8.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1nv8| PDB=1nv8 | SCENE= }}
{{STRUCTURE_1nv8| PDB=1nv8 | SCENE= }}
-
'''N5-glutamine methyltransferase, HemK'''
+
===N5-glutamine methyltransferase, HemK===
-
==Overview==
+
<!--
-
Posttranslational methylation of release factors on the glutamine residue of a conserved GGQ motif is required for efficient termination of protein synthesis. This methylation is performed by an N(5)-glutamine methyltransferase called PrmC/HemK, whose crystal structure we report here at 2.2 A resolution. The electron density at the active site appears to contain a mixture of the substrates, S-adenosyl-L-methionine (AdoMet) and glutamine, and the products, S-adenosyl-L-homocysteine (AdoHcy) and N(5)-methylglutamine. The C-terminal domain of PrmC adopts the canonical AdoMet-dependent methyltransferase fold and shares structural similarity with the nucleotide N-methyltransferases in the active site, including use of a conserved (D/N)PPY motif to select and position the glutamine substrate. Residues of the PrmC (197)NPPY(200) motif form hydrogen bonds that position the planar Gln side chain such that the lone-pair electrons on the nitrogen nucleophile are oriented toward the methyl group of AdoMet. In the product complex, the methyl group remains pointing toward the sulfur, consistent with either an sp(3)-hybridized, positively charged Gln nitrogen, or a neutral sp(2)-hybridized nitrogen in a strained conformation. Due to steric overlap within the active site, proton loss and formation of the neutral planar methylamide product are likely to occur during or after product release. These structures, therefore, represent intermediates along the catalytic pathway of PrmC and show how the (D/N)PPY motif can be used to select a wide variety substrates.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12741815}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12741815 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12741815}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Schubert, H L.]]
[[Category: Schubert, H L.]]
[[Category: Class i adomet-dependent methyltransferase]]
[[Category: Class i adomet-dependent methyltransferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:01:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:42:03 2008''

Revision as of 03:42, 28 July 2008

Image:1nv8.png

Template:STRUCTURE 1nv8

N5-glutamine methyltransferase, HemK

Template:ABSTRACT PUBMED 12741815

About this Structure

1NV8 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Structures along the catalytic pathway of PrmC/HemK, an N5-glutamine AdoMet-dependent methyltransferase., Schubert HL, Phillips JD, Hill CP, Biochemistry. 2003 May 20;42(19):5592-9. PMID:12741815

Page seeded by OCA on Mon Jul 28 06:42:03 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nv8"
Personal tools