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.


1p0y

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1p0y.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1p0y.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1p0y| PDB=1p0y | SCENE= }}
{{STRUCTURE_1p0y| PDB=1p0y | SCENE= }}
-
'''Crystal structure of the SET domain of LSMT bound to MeLysine and AdoHcy'''
+
===Crystal structure of the SET domain of LSMT bound to MeLysine and AdoHcy===
-
==Overview==
+
<!--
-
SET domain protein methyltransferases catalyze the transfer of methyl groups from the cofactor S-adenosylmethionine (AdoMet) to specific lysine residues of protein substrates, such as the N-terminal tails of histones H3 and H4 and the large subunit of the Rubisco holoenzyme complex. The crystal structures of pea Rubisco large subunit methyltransferase (LSMT) in ternary complexes with either lysine or epsilon-N-methyllysine (MeLys) and the product S-adenosylhomocysteine (AdoHcy) were determined to resolutions of 2.65 and 2.55 A, respectively. The zeta-methyl group of MeLys is bound to the enzyme via carbon-oxygen hydrogen bonds that play a key role in catalysis. The methyl donor and acceptor are aligned in a linear geometry for S(N)2 nucleophilic transfer of the methyl group during catalysis. Differences in hydrogen bonding between the MeLys epsilon-amino group and Rubisco LSMT and SET7/9 explain why Rubisco LSMT generates multiply methylated Lys, wheras SET7/9 generates only MeLys.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12819771}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12819771 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12819771}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Post-translational modification]]
[[Category: Post-translational modification]]
[[Category: Set domain]]
[[Category: Set domain]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:32:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:52:41 2008''

Revision as of 08:52, 28 July 2008

Image:1p0y.png

Template:STRUCTURE 1p0y

Crystal structure of the SET domain of LSMT bound to MeLysine and AdoHcy

Template:ABSTRACT PUBMED 12819771

About this Structure

1P0Y is a Single protein structure of sequence from Pisum sativum. Full crystallographic information is available from OCA.

Reference

Mechanism of multiple lysine methylation by the SET domain enzyme Rubisco LSMT., Trievel RC, Flynn EM, Houtz RL, Hurley JH, Nat Struct Biol. 2003 Jul;10(7):545-52. PMID:12819771

Page seeded by OCA on Mon Jul 28 11:52:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p0y"
Personal tools