1yub

From Proteopedia

(Difference between revisions)

Revision as of 07:13, 2 March 2022

SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, MINIMIZED AVERAGE STRUCTURE

Structural highlights

1yub is a 1 chain structure with sequence from "diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	ERM ("Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886)
Activity:	Transferase, with EC number 2.1.1.182, 2.1.1.183 and 2.1.1.184 2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ERM_STREE] 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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The Erm family of methyltransferases is responsible for the development of resistance to the macrolide-lincosamide-streptogramin type B (MLS) antibiotics. These enzymes methylate an adenine of 23S ribosomal RNA that prevents the MLS antibiotics from binding to the ribosome and exhibiting their antibacterial activity. Here we describe the three-dimensional structure of an Erm family member, ErmAM, as determined by NMR spectroscopy. The catalytic domain of ErmAM is structurally similar to that found in other methyltransferases and consists of a seven-stranded beta-sheet flanked by alpha-helices and a small two-stranded beta-sheet. In contrast to the catalytic domain, the substrate binding domain is different from other methyltransferases and adopts a novel fold that consists of four alpha-helices.

Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance.,Yu L, Petros AM, Schnuchel A, Zhong P, Severin JM, Walter K, Holzman TF, Fesik SW Nat Struct Biol. 1997 Jun;4(6):483-9. PMID:9187657^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Yu L, Petros AM, Schnuchel A, Zhong P, Severin JM, Walter K, Holzman TF, Fesik SW. Solution structure of an rRNA methyltransferase (ErmAM) that confers macrolide-lincosamide-streptogramin antibiotic resistance. Nat Struct Biol. 1997 Jun;4(6):483-9. PMID:9187657

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yub"

@@ Line 3: / Line 3: @@
 <StructureSection load='1yub' size='340' side='right'caption='[[1yub]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1yub]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YUB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1yub]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"diplococcus_pneumoniae"_(klein_1884)_weichselbaum_1886 "diplococcus pneumoniae" (klein 1884) weichselbaum 1886]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YUB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YUB FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 "Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1313 "Diplococcus pneumoniae" (Klein 1884) Weichselbaum 1886])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184 2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Transferase Transferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184 2.1.1.181, 2.1.1.182, 2.1.1.183 and 2.1.1.184] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1yub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yub OCA], [http://pdbe.org/1yub PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yub RCSB], [http://www.ebi.ac.uk/pdbsum/1yub PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yub ProSAT]</span></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=1yub FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yub OCA], [https://pdbe.org/1yub PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yub RCSB], [https://www.ebi.ac.uk/pdbsum/1yub PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yub ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ERM_STREE ERM_STREE]] 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.
+[[https://www.uniprot.org/uniprot/ERM_STREE ERM_STREE]] 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1yub

From Proteopedia

Revision as of 07:13, 2 March 2022

SOLUTION STRUCTURE OF AN RRNA METHYLTRANSFERASE (ERMAM) THAT CONFERS MACROLIDE-LINCOSAMIDE-STREPTOGRAMIN ANTIBIOTIC RESISTANCE, NMR, MINIMIZED AVERAGE STRUCTURE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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