1njm: Difference between revisions

Revision as of 21:18, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1njm.png

Template:STRUCTURE 1njm

The crystal structure of the 50S Large ribosomal subunit from Deinococcus radiodurans complexed with a tRNA acceptor stem mimic (ASM) and the antibiotic sparsomycinThe crystal structure of the 50S Large ribosomal subunit from Deinococcus radiodurans complexed with a tRNA acceptor stem mimic (ASM) and the antibiotic sparsomycin

Template:ABSTRACT PUBMED 12535524

About this StructureAbout this Structure

1NJM is a Protein complex structure of sequences from Deinococcus radiodurans. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression., Bashan A, Agmon I, Zarivach R, Schluenzen F, Harms J, Berisio R, Bartels H, Franceschi F, Auerbach T, Hansen HA, Kossoy E, Kessler M, Yonath A, Mol Cell. 2003 Jan;11(1):91-102. PMID:12535524

Page seeded by OCA on Mon Jul 28 21:18:20 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1njm.gif|left|200px]]
+{{Seed}}
+[[Image:1njm.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1njm|  PDB=1njm  |  SCENE=  }}
-'''The crystal structure of the 50S Large ribosomal subunit from Deinococcus radiodurans complexed with a tRNA acceptor stem mimic (ASM) and the antibiotic sparsomycin'''
+===The crystal structure of the 50S Large ribosomal subunit from Deinococcus radiodurans complexed with a tRNA acceptor stem mimic (ASM) and the antibiotic sparsomycin===
-==Overview==
+<!--
-Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3' end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this mechanism.
+The line below this paragraph, {{ABSTRACT_PUBMED_12535524}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12535524 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12535524}}
 ==About this Structure==
@@ Line 37: / Line 41: @@
 [[Category: Sparsomycin]]
 [[Category: Trna]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 02:36:37 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 21:18:20 2008''