1v2a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:43, 25 October 2023) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1v2a.png|left|200px]]
 
-
<!--
+
==Glutathione S-transferase 1-6 from Anopheles dirus species B==
-
The line below this paragraph, containing "STRUCTURE_1v2a", creates the "Structure Box" on the page.
+
<StructureSection load='1v2a' size='340' side='right'caption='[[1v2a]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1v2a]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Anopheles_dirus Anopheles dirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V2A FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GTS:GLUTATHIONE+SULFONIC+ACID'>GTS</scene></td></tr>
-
{{STRUCTURE_1v2a| PDB=1v2a | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v2a OCA], [https://pdbe.org/1v2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v2a RCSB], [https://www.ebi.ac.uk/pdbsum/1v2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v2a ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/Q9BHB0_9DIPT Q9BHB0_9DIPT]
 +
== 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/v2/1v2a_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=1v2a ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The insect GST (glutathione transferase) supergene family encodes a varied group of proteins belonging to at least six individual classes. Interest in insect GSTs has focused on their role in conferring insecticide resistance. Previously from the mosquito malaria vector Anopheles dirus, two genes encoding five Delta class GSTs have been characterized for structural as well as enzyme activities. We have obtained a new Delta class GST gene and isoenzyme from A. dirus, which we name adGSTD5-5. The adGSTD5-5 isoenzyme was identified and was only detectably expressed in A. dirus adult females. A putative promoter analysis suggests that this GST has an involvement in oogenesis. The enzyme displayed little activity for classical GST substrates, although it possessed the greatest activity for DDT [1,1,1-trichloro-2,2-bis-(p-chlorophenyl)ethane] observed for Delta GSTs. However, GST activity was inhibited or enhanced in the presence of various fatty acids, suggesting that the enzyme may be modulated by fatty acids. We obtained a crystal structure for adGSTD5-5 and compared it with other Delta GSTs, which showed that adGSTD5-5 possesses an elongated and more polar active-site topology.
-
===Glutathione S-transferase 1-6 from Anopheles dirus species B===
+
Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme.,Udomsinprasert R, Pongjaroenkit S, Wongsantichon J, Oakley AJ, Prapanthadara LA, Wilce MC, Ketterman AJ Biochem J. 2005 Jun 15;388(Pt 3):763-71. PMID:15717864<ref>PMID:15717864</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1v2a" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_15717864}}, adds the Publication Abstract to the page
+
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 15717864 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_15717864}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
-
1V2A is a 4 chains structure of sequences from [http://en.wikipedia.org/wiki/Anopheles_dirus Anopheles dirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V2A OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:15717864</ref><references group="xtra"/>
+
[[Category: Anopheles dirus]]
[[Category: Anopheles dirus]]
-
[[Category: Glutathione transferase]]
+
[[Category: Large Structures]]
-
[[Category: Oakley, A J.]]
+
[[Category: Oakley AJ]]
-
[[Category: Detoxification]]
+
-
[[Category: Glutathione]]
+
-
[[Category: Glutathione s-transferase]]
+
-
[[Category: Xenobiotic]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 00:06:32 2009''
+

Current revision

Glutathione S-transferase 1-6 from Anopheles dirus species B

PDB ID 1v2a

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/1v2a"
Personal tools