This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1ah9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ah9.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ah9.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ah9| PDB=1ah9 | SCENE= }}
{{STRUCTURE_1ah9| PDB=1ah9 | SCENE= }}
-
'''THE STRUCTURE OF THE TRANSLATIONAL INITIATION FACTOR IF1 FROM ESCHERICHIA COLI, NMR, 19 STRUCTURES'''
+
===THE STRUCTURE OF THE TRANSLATIONAL INITIATION FACTOR IF1 FROM ESCHERICHIA COLI, NMR, 19 STRUCTURES===
-
==Overview==
+
<!--
-
The structure of the translational initiation factor IF1 from Escherichia coli has been determined with multidimensional NMR spectroscopy. Using 1041 distance and 78 dihedral constraints, 40 distance geometry structures were calculated, which were refined by restrained molecular dynamics. From this set, 19 structures were selected, having low constraint energy and few constraint violations. The ensemble of 19 structures displays a root-mean-square deviation versus the average of 0.49 A for the backbone atoms and 1.12 A for all atoms for residues 6-36 and 46-67. The structure of IF1 is characterized by a five-stranded beta-barrel. The loop connecting strands three and four contains a short 3(10) helix but this region shows considerably higher flexibility than the beta-barrel. The fold of IF1 is very similar to that found in the bacterial cold shock proteins CspA and CspB, the N-terminal domain of aspartyl-tRNA synthetase and the staphylococcal nuclease, and can be identified as the oligomer-binding motif. Several proteins of this family are nucleic acid-binding proteins. This suggests that IF1 plays its role in the initiation of protein synthesis by nucleic acid interactions. Specific changes of NMR signals of IF1 upon titration with 30S ribosomal subunit identifies several residues that are involved in the interaction with ribosomes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9135158}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9135158 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9135158}}
==About this Structure==
==About this Structure==
-
1AH9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AH9 OCA].
+
1AH9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AH9 OCA].
==Reference==
==Reference==
Line 32: Line 36:
[[Category: Protein-rna interaction]]
[[Category: Protein-rna interaction]]
[[Category: Ribosome binding]]
[[Category: Ribosome binding]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:16:08 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:50:52 2008''

Revision as of 13:50, 30 June 2008

Image:1ah9.png

Template:STRUCTURE 1ah9

THE STRUCTURE OF THE TRANSLATIONAL INITIATION FACTOR IF1 FROM ESCHERICHIA COLI, NMR, 19 STRUCTURES

Template:ABSTRACT PUBMED 9135158

About this Structure

1AH9 is a Single protein structure of sequence from Escherichia coli. Full experimental information is available from OCA.

Reference

The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif., Sette M, van Tilborg P, Spurio R, Kaptein R, Paci M, Gualerzi CO, Boelens R, EMBO J. 1997 Mar 17;16(6):1436-43. PMID:9135158

Page seeded by OCA on Mon Jun 30 16:50:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ah9"
Personal tools