1qao: Difference between revisions
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[[Image:1qao.jpg|left|200px]] | [[Image:1qao.jpg|left|200px]] | ||
'''THE STRUCTURE OF THE RRNA METHYLTRANSFERASE ERMC': IMPLICATIONS FOR THE REACTION MECHANISM''' | {{Structure | ||
|PDB= 1qao |SIZE=350|CAPTION= <scene name='initialview01'>1qao</scene>, resolution 2.7Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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== | ||
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==About this Structure== | ==About this Structure== | ||
1QAO is a [ | 1QAO 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=1QAO 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:// | 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]] | ||
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[[Category: binary complex with s-adenosylmethionine]] | [[Category: binary complex with s-adenosylmethionine]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''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
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| 1qao, resolution 2.7Å | |||||||||||||
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| Ligands: | SAM | ||||||||||||
| 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
1QAO 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
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