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.


1mea

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1mea.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1mea.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1mea| PDB=1mea | SCENE= }}
{{STRUCTURE_1mea| PDB=1mea | SCENE= }}
-
'''METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS'''
+
===METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS===
-
==Overview==
+
<!--
-
Methionyl-tRNA synthetase from Escherichia coli contains one tightly bound zinc atom per subunit. The region encompassing residues 138 to 163 of this enzyme is responsible for the metal binding. A 28-mer peptide corresponding to these residues was expressed in vivo and shown to contain approximately 1 mol of tightly bound Zn/mol of peptide. In this study, the three-dimensional solution structure of this peptide was solved by means of two-dimensional proton NMR spectroscopy. A total of 133 nuclear Overhauser effect distance constraints and 22 dihedral angle restraints were used for the calculations, using a hybrid distance-geometry-simulated annealing strategy. Excluding the first four residues, the resulting structure is well-defined (r.m.s.d. 0.71 A for backbone atoms) and composed of a series of four tight turns. The second and the fourth turns are composed of CXXC sequences which are structurally homologous to the NH-S turns found in the metal binding sites of gag retroviral proteins and rubredoxin. The solution structure of the zinc binding peptide shows significant discrepancies with the crystal structure of methionyl-tRNA synthetase.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8515466}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8515466 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8515466}}
==About this Structure==
==About this Structure==
-
1MEA 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=1MEA OCA].
+
1MEA 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=1MEA OCA].
==Reference==
==Reference==
Line 26: Line 30:
[[Category: Fourmy, D.]]
[[Category: Fourmy, D.]]
[[Category: Aminoacyl-trna synthase]]
[[Category: Aminoacyl-trna synthase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:56:17 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:47:06 2008''

Revision as of 20:47, 2 July 2008

Template:STRUCTURE 1mea

METHIONYL-TRNA SYNTHETASE ZINC BINDING DOMAIN. 3D STRUCTURE AND HOMOLOGY WITH RUBREDOXIN AND GAG RETROVIRAL PROTEINS

Template:ABSTRACT PUBMED 8515466

About this Structure

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

Reference

Methionyl-tRNA synthetase zinc binding domain. Three-dimensional structure and homology with rubredoxin and gag retroviral proteins., Fourmy D, Dardel F, Blanquet S, J Mol Biol. 1993 Jun 20;231(4):1078-89. PMID:8515466

Page seeded by OCA on Wed Jul 2 23:47:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools