2erc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:19, 14 February 2024) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:2erc.jpg|left|200px]]
 
-
<!--
+
==CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE==
-
The line below this paragraph, containing "STRUCTURE_2erc", creates the "Structure Box" on the page.
+
<StructureSection load='2erc' size='340' side='right'caption='[[2erc]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[2erc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ERC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ERC FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.03&#8491;</td></tr>
-
-->
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2erc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2erc OCA], [https://pdbe.org/2erc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2erc RCSB], [https://www.ebi.ac.uk/pdbsum/2erc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2erc ProSAT]</span></td></tr>
-
{{STRUCTURE_2erc| PDB=2erc | SCENE= }}
+
</table>
-
 
+
== Function ==
-
'''CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE'''
+
[https://www.uniprot.org/uniprot/ERM_BACIU ERM_BACIU] This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.<ref>PMID:12907737</ref> <ref>PMID:12946350</ref>
-
 
+
== Evolutionary Conservation ==
-
 
+
[[Image:Consurf_key_small.gif|200px|right]]
-
==Overview==
+
Check<jmol>
-
The prevalent mechanism of bacterial resistance to erythromycin and other antibiotics of the macrolide-lincosamide-streptogramin B group (MLS) is methylation of the 23S rRNA component of the 50S subunit in bacterial ribosomes. This sequence-specific methylation is catalyzed by the Erm group of methyltransferases (MTases). They are found in several strains of pathogenic bacteria, and ErmC is the most studied member of this class. The crystal structure of ErmC' (a naturally occurring variant of ErmC) from Bacillus subtilis has been determined at 3.0 A resolution by multiple anomalous diffraction phasing methods. The structure consists of a conserved alpha/beta amino-terminal domain which binds the cofactor S-adenosyl-l-methionine (SAM), followed by a smaller, alpha-helical RNA-recognition domain. The beta-sheet structure of the SAM-binding domain is well-conserved between the DNA, RNA, and small-molecule MTases. However, the C-terminal nucleic acid binding domain differs from the DNA-binding domains of other MTases and is unlike any previously reported RNA-recognition fold. A large, positively charged, concave surface is found at the interface of the N- and C-terminal domains and is proposed to form part of the protein-RNA interaction surface. ErmC' exhibits the conserved structural motifs previously found in the SAM-binding domain of other methyltransferases. A model of SAM bound to ErmC' is presented which is consistent with the motif conservation among MTases.
+
<jmolCheckbox>
-
 
+
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/2erc_consurf.spt"</scriptWhenChecked>
-
==About this Structure==
+
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
-
2ERC 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=2ERC OCA].
+
<text>to colour the structure by Evolutionary Conservation</text>
-
 
+
</jmolCheckbox>
-
==Reference==
+
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2erc ConSurf].
-
Crystal structure of ErmC', an rRNA methyltransferase which mediates antibiotic resistance in bacteria., Bussiere DE, Muchmore SW, Dealwis CG, Schluckebier G, Nienaber VL, Edalji RP, Walter KA, Ladror US, Holzman TF, Abad-Zapatero C, Biochemistry. 1998 May 19;37(20):7103-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9585521 9585521]
+
<div style="clear:both"></div>
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Abad-Zapatero, C.]]
+
[[Category: Abad-Zapatero C]]
-
[[Category: Bussiere, D E.]]
+
[[Category: Bussiere DE]]
-
[[Category: Dealwis, C G.]]
+
[[Category: Dealwis CG]]
-
[[Category: Muchmore, S W.]]
+
[[Category: Muchmore SW]]
-
[[Category: Schluckebier, G.]]
+
[[Category: Schluckebier G]]
-
[[Category: Antibiotic resistance]]
+
-
[[Category: Erythromycin resistance methylase cs']]
+
-
[[Category: Methyltransferase]]
+
-
[[Category: Rrna methyltransferase]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:01:51 2008''
+

Current revision

CRYSTAL STRUCTURE OF ERMC' A RRNA-METHYL TRANSFERASE

PDB ID 2erc

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2erc"
Personal tools