1k01

From Proteopedia

(Difference between revisions)

Revision as of 09:25, 6 November 2019

Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria

Structural highlights

1k01 is a 4 chain structure with sequence from Deinococcus radiodurans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	1jzx, 1jzy, 1jzz, 1k00
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RL32_DEIRA] Forms a cluster with L17 and L22, and with L22, a pair of "tweezers" that hold together all the domains of the 23S rRNA. Interacts with the antibiotic troleandomycin which blocks the peptide exit tunnel.[HAMAP-Rule:MF_00340] [RL22_DEIRA] This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (By similarity).[HAMAP-Rule:MF_01331_B] The globular domain of the protein is located by the polypeptide exit tunnel on the outside of the subunit while an extended beta-hairpin forms part of the wall of the tunnel. Forms a pair of "tweezers" with L32 that hold together two different domains of the 23S rRNA. Interacts with the tunnel-blocking modified macrolide azithromycin. Upon binding of the macrolide troleadomycin to the ribosome, the tip of the beta-hairpin is displaced, which severely restricts the tunnel. This and experiments in E.coli have led to the suggestion that it is part of the gating mechanism involved in translation arrest in the absence of the protein export system.[HAMAP-Rule:MF_01331_B] [RL4_DEIRA] One of the primary rRNA binding proteins, this protein initially binds near the 5'-end of the 23S rRNA. It is important during the early stages of 50S assembly (By similarity).[HAMAP-Rule:MF_01328_B] Makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit.[HAMAP-Rule:MF_01328_B] This protein is located close to the polypeptide exit tunnel, and interacts with the modified macrolide azithromycin, which blocks the tunnel.[HAMAP-Rule:MF_01328_B]

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

Ribosomes, the site of protein synthesis, are a major target for natural and synthetic antibiotics. Detailed knowledge of antibiotic binding sites is central to understanding the mechanisms of drug action. Conversely, drugs are excellent tools for studying the ribosome function. To elucidate the structural basis of ribosome-antibiotic interactions, we determined the high-resolution X-ray structures of the 50S ribosomal subunit of the eubacterium Deinococcus radiodurans, complexed with the clinically relevant antibiotics chloramphenicol, clindamycin and the three macrolides erythromycin, clarithromycin and roxithromycin. We found that antibiotic binding sites are composed exclusively of segments of 23S ribosomal RNA at the peptidyl transferase cavity and do not involve any interaction of the drugs with ribosomal proteins. Here we report the details of antibiotic interactions with the components of their binding sites. Our results also show the importance of putative Mg+2 ions for the binding of some drugs. This structural analysis should facilitate rational drug design.

Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria.,Schlunzen F, Zarivach R, Harms J, Bashan A, Tocilj A, Albrecht R, Yonath A, Franceschi F Nature. 2001 Oct 25;413(6858):814-21. PMID:11677599^[1]

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

References

↑ Schlunzen F, Zarivach R, Harms J, Bashan A, Tocilj A, Albrecht R, Yonath A, Franceschi F. Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature. 2001 Oct 25;413(6858):814-21. PMID:11677599 doi:http://dx.doi.org/10.1038/35101544

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k01"

@@ Line 1: / Line 1: @@
 ==Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria==
-<StructureSection load='1k01' size='340' side='right' caption='[[1k01]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
+<StructureSection load='1k01' size='340' side='right'caption='[[1k01]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1k01]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K01 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K01 FirstGlance]. <br>
@@ Line 30: / Line 30: @@
 </div>
 <div class="pdbe-citations 1k01" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Ribosomal protein L22|Ribosomal protein L22]]
+*[[Ribosomal protein L32|Ribosomal protein L32]]
+*[[Ribosomal protein L4|Ribosomal protein L4]]
 == References ==
 <references/>
@@ Line 35: / Line 40: @@
 </StructureSection>
 [[Category: Deinococcus radiodurans]]
+[[Category: Large Structures]]
 [[Category: Albrecht, R]]
 [[Category: Bashan, A]]
@@ Line 43: / Line 49: @@
 [[Category: Yonath, A]]
 [[Category: Zarivach, R]]
-[[Category: 5]]
 [[Category: Antibiotic]]
 [[Category: Chloramphenicol]]
 [[Category: Peptidyl transferase center]]
 [[Category: Ribosome]]

1k01

From Proteopedia

Revision as of 09:25, 6 November 2019

Structural Basis for the Interaction of Antibiotics with the Peptidyl Transferase Center in Eubacteria

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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