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.


1qan

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qan.jpg|left|200px]]<br /><applet load="1qan" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1qan.jpg|left|200px]]
-
caption="1qan, resolution 2.4&Aring;" />
+
 
-
'''THE STRUCTURE OF THE RRNA METHYLTRANSFERASE ERMC': IMPLICATIONS FOR THE REACTION MECHANISM'''<br />
+
{{Structure
 +
|PDB= 1qan |SIZE=350|CAPTION= <scene name='initialview01'>1qan</scene>, resolution 2.4&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene> and <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/rRNA_(adenine-N(6)-)-methyltransferase rRNA (adenine-N(6)-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.48 2.1.1.48]
 +
|GENE=
 +
}}
 +
 
 +
'''THE STRUCTURE OF THE RRNA METHYLTRANSFERASE ERMC': IMPLICATIONS FOR THE REACTION MECHANISM'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1QAN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=SAH:'>SAH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/rRNA_(adenine-N(6)-)-methyltransferase rRNA (adenine-N(6)-)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.48 2.1.1.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAN OCA].
+
1QAN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QAN OCA].
==Reference==
==Reference==
-
The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism., Schluckebier G, Zhong P, Stewart KD, Kavanaugh TJ, Abad-Zapatero C, J Mol Biol. 1999 Jun 4;289(2):277-91. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10366505 10366505]
+
The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism., Schluckebier G, Zhong P, Stewart KD, Kavanaugh TJ, Abad-Zapatero C, J Mol Biol. 1999 Jun 4;289(2):277-91. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10366505 10366505]
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 23: Line 32:
[[Category: binary complex with s-adenosyl-homocysteine]]
[[Category: binary complex with s-adenosyl-homocysteine]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:37 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:35:10 2008''

Revision as of 11:35, 20 March 2008


PDB ID 1qan

Drag the structure with the mouse to rotate
, resolution 2.4Å
Ligands: and
Activity: rRNA (adenine-N(6)-)-methyltransferase, with EC number 2.1.1.48
Coordinates: save as pdb, mmCIF, xml



THE STRUCTURE OF THE RRNA METHYLTRANSFERASE ERMC': IMPLICATIONS FOR THE REACTION MECHANISM


Overview

The rRNA methyltransferase ErmC' transfers methyl groups from S -adenosyl-l-methionine to atom N6 of an adenine base within the peptidyltransferase loop of 23 S rRNA, thus conferring antibiotic resistance against a number of macrolide antibiotics. The crystal structures of ErmC' and of its complexes with the cofactor S -adenosyl-l-methionine, the reaction product S-adenosyl-l-homocysteine and the methyltransferase inhibitor Sinefungin, respectively, show that the enzyme undergoes small conformational changes upon ligand binding. Overall, the ligand molecules bind to the protein in a similar mode as observed for other methyltransferases. Small differences between the binding of the amino acid parts of the different ligands are correlated with differences in their chemical structure. A model for the transition-state based on the atomic details of the active site is consistent with a one-step methyl-transfer mechanism and might serve as a first step towards the design of potent Erm inhibitors.

About this Structure

1QAN is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism., Schluckebier G, Zhong P, Stewart KD, Kavanaugh TJ, Abad-Zapatero C, J Mol Biol. 1999 Jun 4;289(2):277-91. PMID:10366505

Page seeded by OCA on Thu Mar 20 13:35:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools