4tmy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:51, 9 August 2023) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:4tmy.jpg|left|200px]]
 
-
{{Structure
+
==CHEY FROM THERMOTOGA MARITIMA (MG-IV)==
-
|PDB= 4tmy |SIZE=350|CAPTION= <scene name='initialview01'>4tmy</scene>, resolution 2.8&Aring;
+
<StructureSection load='4tmy' size='340' side='right'caption='[[4tmy]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=ACA:Active+Site+And+Metal+Binding+Site'>ACA</scene> and <scene name='pdbsite=ACB:Active+Site+And+Metal+Binding+Site'>ACB</scene>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
+
<table><tr><td colspan='2'>[[4tmy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TMY 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]] 2.8&#8491;</td></tr>
-
|GENE= CHEY ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=4tmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tmy OCA], [https://pdbe.org/4tmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tmy RCSB], [https://www.ebi.ac.uk/pdbsum/4tmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tmy ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CHEY_THEMA CHEY_THEMA] Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheY seems to regulate the clockwise (CW) rotation (By similarity).
 +
== 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/tm/4tmy_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=4tmy ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The crystal structure of CheY protein from Thermotoga maritima has been determined in four crystal forms with and without Mg++ bound, at up to 1.9 A resolution. Structural comparisons with CheY from Escherichia coli shows substantial similarity in their folds, with some concerted changes propagating away from the active site that suggest how phosphorylated CheY, a signal transduction protein in bacterial chemotaxis, is recognized by its targets. A highly conserved segment of the protein (the "y-turn loop," residues 55-61), previously suggested to be a rigid recognition determinant, is for the first time seen in two alternative conformations in the different crystal structures. Although CheY from Thermotoga has much higher thermal stability than its mesophilic counterparts, comparison of structural features previously proposed to enhance thermostability such as hydrogen bonds, ion pairs, compactness, and hydrophobic surface burial would not suggest it to be so.
-
'''CHEY FROM THERMOTOGA MARITIMA (MG-IV)'''
+
Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability.,Usher KC, de la Cruz AF, Dahlquist FW, Swanson RV, Simon MI, Remington SJ Protein Sci. 1998 Feb;7(2):403-12. PMID:9521117<ref>PMID:9521117</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 4tmy" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
The crystal structure of CheY protein from Thermotoga maritima has been determined in four crystal forms with and without Mg++ bound, at up to 1.9 A resolution. Structural comparisons with CheY from Escherichia coli shows substantial similarity in their folds, with some concerted changes propagating away from the active site that suggest how phosphorylated CheY, a signal transduction protein in bacterial chemotaxis, is recognized by its targets. A highly conserved segment of the protein (the "y-turn loop," residues 55-61), previously suggested to be a rigid recognition determinant, is for the first time seen in two alternative conformations in the different crystal structures. Although CheY from Thermotoga has much higher thermal stability than its mesophilic counterparts, comparison of structural features previously proposed to enhance thermostability such as hydrogen bonds, ion pairs, compactness, and hydrophobic surface burial would not suggest it to be so.
+
*[[Chemotaxis protein 3D structures|Chemotaxis protein 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
4TMY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TMY OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
[[Category: Large Structures]]
-
Crystal structures of CheY from Thermotoga maritima do not support conventional explanations for the structural basis of enhanced thermostability., Usher KC, de la Cruz AF, Dahlquist FW, Swanson RV, Simon MI, Remington SJ, Protein Sci. 1998 Feb;7(2):403-12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9521117 9521117]
+
-
[[Category: Single protein]]
+
[[Category: Thermotoga maritima]]
[[Category: Thermotoga maritima]]
-
[[Category: Cruz, A De La.]]
+
[[Category: Dahlquist FW]]
-
[[Category: Dahlquist, F W.]]
+
[[Category: De La Cruz A]]
-
[[Category: Remington, S J.]]
+
[[Category: Remington SJ]]
-
[[Category: Usher, K C.]]
+
[[Category: Usher KC]]
-
[[Category: MG]]
+
-
[[Category: chemotaxis]]
+
-
[[Category: magnesium binding]]
+
-
[[Category: phosphoryl transfer]]
+
-
[[Category: signal transduction]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:11:15 2008''
+

Current revision

CHEY FROM THERMOTOGA MARITIMA (MG-IV)

PDB ID 4tmy

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools