1qaq
From Proteopedia
(New page: 200px<br /><applet load="1qaq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qaq, resolution 2.8Å" /> '''THE STRUCTURE OF THE ...) |
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| - | [[Image:1qaq.jpg|left|200px]]<br /><applet load="1qaq" size=" | + | [[Image:1qaq.jpg|left|200px]]<br /><applet load="1qaq" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qaq, resolution 2.8Å" /> | caption="1qaq, resolution 2.8Å" /> | ||
'''THE STRUCTURE OF THE RRNA METHYLTRANSFERASE ERMC': IMPLICATIONS FOR THE REACTION MECHANISM'''<br /> | '''THE STRUCTURE OF THE RRNA METHYLTRANSFERASE ERMC': IMPLICATIONS FOR THE REACTION MECHANISM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The rRNA methyltransferase ErmC' transfers methyl groups from S | + | 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== | ==About this Structure== | ||
| - | 1QAQ 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 SFG as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1QAQ 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=SFG:'>SFG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1QAQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: binary complex with adenosyl-ornithine]] | [[Category: binary complex with adenosyl-ornithine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:37:41 2008'' |
Revision as of 12:37, 21 February 2008
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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
1QAQ is a Single protein structure of sequence from Bacillus subtilis with as ligand. Active as rRNA (adenine-N(6)-)-methyltransferase, with EC number 2.1.1.48 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
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