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.


1dg1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:53, 7 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1dg1.gif|left|200px]]
 
-
{{Structure
+
==WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).==
-
|PDB= 1dg1 |SIZE=350|CAPTION= <scene name='initialview01'>1dg1</scene>, resolution 2.50&Aring;
+
<StructureSection load='1dg1' size='340' side='right'caption='[[1dg1]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>
+
<table><tr><td colspan='2'>[[1dg1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DG1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DG1 FirstGlance]. <br>
-
|ACTIVITY=
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=1dg1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dg1 OCA], [https://pdbe.org/1dg1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dg1 RCSB], [https://www.ebi.ac.uk/pdbsum/1dg1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dg1 ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/EFTU2_ECOLI EFTU2_ECOLI] This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.[HAMAP-Rule:MF_00118] May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.[HAMAP-Rule:MF_00118]
 +
== 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/dg/1dg1_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=1dg1 ConSurf].
 +
<div style="clear:both"></div>
-
'''WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).'''
+
==See Also==
-
 
+
*[[Elongation factor 3D structures|Elongation factor 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
BACKGROUND: The bacterial elongation factor EF-Tu recognizes and transports aminoacyl-tRNAs to mRNA-programmed ribosomes. EF-Tu shares many structural and functional properties with other GTPases whose conformations are regulated by guanine nucleotides. RESULTS: An intact form of Escherichia coli EF-Tu complexed with GDP has been crystallized in the presence of the EF-Tu-specific antibiotic GE2270 A. The three-dimensional structure has been solved by X-ray diffraction analysis and refined to a final crystallographic R factor of 17.2% at a resolution of 2.5 A. The location of the GE2270 A antibiotic-binding site could not be identified. CONCLUSIONS: The structure of EF-Tu-GDP is nearly identical to that of a trypsin-modified form of EF-Tu-GDP, demonstrating conclusively that the protease treatment had not altered any essential structural features. The present structure represents the first view of an ordered Switch I region in EF-Tu-GDP and reveals similarities with two other GTPases complexed with GDP: Ran and ADP-ribosylation factor-1. A comparison of the Switch I regions of the GTP and GDP forms of EF-Tu also reveals that a segment, six amino acids in length, completely converts from an alpha helix in the GTP complex to beta secondary structure in the GDP form. The alpha to beta switch in EF-Tu may represent a prototypical activation mechanism for other protein families.
+
-
 
+
-
==About this Structure==
+
-
1DG1 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=1DG1 OCA].
+
-
 
+
-
==Reference==
+
-
An alpha to beta conformational switch in EF-Tu., Abel K, Yoder MD, Hilgenfeld R, Jurnak F, Structure. 1996 Oct 15;4(10):1153-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8939740 8939740]
+
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Abel, K.]]
+
[[Category: Abel K]]
-
[[Category: Hilgenfeld, R.]]
+
[[Category: Hilgenfeld R]]
-
[[Category: Jurnak, F.]]
+
[[Category: Jurnak F]]
-
[[Category: Yoder, M.]]
+
[[Category: Yoder M]]
-
[[Category: GDP]]
+
-
[[Category: MG]]
+
-
[[Category: alpha beta shift]]
+
-
[[Category: elongation factor]]
+
-
[[Category: gdp binding]]
+
-
[[Category: gtpase]]
+
-
[[Category: trna binding]]
+
-
[[Category: ts binding protein]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:37:58 2008''
+

Current revision

WHOLE, UNMODIFIED, EF-TU(ELONGATION FACTOR TU).

PDB ID 1dg1

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1dg1"
Personal tools