1ati

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:33, 7 February 2024) (edit) (undo)
 
(21 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1ati.jpg|left|200px]]<br /><applet load="1ati" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1ati, resolution 2.75&Aring;" />
 
-
'''CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS'''<br />
 
-
==Overview==
+
==CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS==
-
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.
+
<StructureSection load='1ati' size='340' side='right'caption='[[1ati]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1ati]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ATI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ATI FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
 +
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ati FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ati OCA], [https://pdbe.org/1ati PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ati RCSB], [https://www.ebi.ac.uk/pdbsum/1ati PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ati ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/SYG_THET8 SYG_THET8] Catalyzes the attachment of glycine to tRNA(Gly) (By similarity).[HAMAP-Rule:MF_00253_B]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/at/1ati_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ati ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ATI OCA].
+
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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]
+
[[Category: Large Structures]]
-
[[Category: Glycine--tRNA ligase]]
+
[[Category: Thermus thermophilus HB8]]
-
[[Category: Single protein]]
+
[[Category: Kern D]]
-
[[Category: Thermus thermophilus]]
+
[[Category: Logan DT]]
-
[[Category: Kern, D.]]
+
[[Category: Mazauric M-H]]
-
[[Category: Logan, D.T.]]
+
[[Category: Moras D]]
-
[[Category: Mazauric, M.H.]]
+
-
[[Category: Moras, D.]]
+
-
[[Category: aminoacyl-trna synthetase]]
+
-
[[Category: ligase]]
+
-
[[Category: protein biosynthesis]]
+
-
[[Category: synthetase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 14:21:27 2007''
+

Current revision

CRYSTAL STRUCTURE OF GLYCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS

PDB ID 1ati

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools