1ati

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ati.jpg|left|200px]]<br /><applet load="1ati" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1ati.jpg|left|200px]]
-
caption="1ati, resolution 2.75&Aring;" />
+
 
-
'''CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS'''<br />
+
{{Structure
 +
|PDB= 1ati |SIZE=350|CAPTION= <scene name='initialview01'>1ati</scene>, resolution 2.75&Aring;
 +
|SITE= <scene name='pdbsite=SA1:These+Residues+Are+Found+To+Be+Responsible+For+On+The+Ba+...'>SA1</scene>
 +
|LIGAND=
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Glycine--tRNA_ligase Glycine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.14 6.1.1.14]
 +
|GENE=
 +
}}
 +
 
 +
'''CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==About this Structure==
==About this Structure==
-
1ATI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/Glycine--tRNA_ligase Glycine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.14 6.1.1.14] Known structural/functional Site: <scene name='pdbsite=SA1:These+Residues+Are+Found+To+Be+Responsible+For+On+The+Ba+...'>SA1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ATI OCA].
+
1ATI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ATI OCA].
==Reference==
==Reference==
-
Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus., Logan DT, Mazauric MH, Kern D, Moras D, EMBO J. 1995 Sep 1;14(17):4156-67. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7556056 7556056]
+
Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus., Logan DT, Mazauric MH, Kern D, Moras D, EMBO J. 1995 Sep 1;14(17):4156-67. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7556056 7556056]
[[Category: Glycine--tRNA ligase]]
[[Category: Glycine--tRNA ligase]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 23: Line 32:
[[Category: synthetase]]
[[Category: synthetase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:10 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:04 2008''

Revision as of 08:02, 20 March 2008


PDB ID 1ati

Drag the structure with the mouse to rotate
, resolution 2.75Å
Sites:
Activity: Glycine--tRNA ligase, with EC number 6.1.1.14
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS


Overview

The sequence and crystal structure at 2.75 A resolution of the homodimeric glycyl-tRNA synthetase from Thermus thermophilus, the first representative of the last unknown class II synthetase subgroup, have been determined. The three class II synthetase sequence motifs are present but the structure was essential for identification of motif 1, which does not possess the proline previously believed to be an essential class II invariant. Nevertheless, crucial contacts with the active site of the other monomer involving motif 1 are conserved and a more comprehensive description of class II now becomes possible. Each monomer consists of an active site strongly resembling that of the aspartyl and seryl enzymes, a C-terminal anticodon recognition domain of 100 residues and a third domain unusually inserted between motifs 1 and 2 almost certainly interacting with the acceptor arm of tRNA(Gly). The C-terminal domain has a novel five-stranded parallel-antiparallel beta-sheet structure with three surrounding helices. The active site residues most probably responsible for substrate recognition, in particular in the Gly binding pocket, can be identified by inference from aspartyl-tRNA synthetase due to the conserved nature of the class II active site.

About this Structure

1ATI is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus., Logan DT, Mazauric MH, Kern D, Moras D, EMBO J. 1995 Sep 1;14(17):4156-67. PMID:7556056

Page seeded by OCA on Thu Mar 20 10:02:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools