3nva

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "3nva" [edit=sysop:move=sysop])
Current revision (16:51, 1 November 2023) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:3nva.png|left|200px]]
 
-
<!--
+
==Dimeric form of CTP synthase from Sulfolobus solfataricus==
-
The line below this paragraph, containing "STRUCTURE_3nva", creates the "Structure Box" on the page.
+
<StructureSection load='3nva' size='340' side='right'caption='[[3nva]], [[Resolution|resolution]] 2.50&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'>[[3nva]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NVA 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]] 2.504&#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=3nva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nva OCA], [https://pdbe.org/3nva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nva RCSB], [https://www.ebi.ac.uk/pdbsum/3nva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nva ProSAT]</span></td></tr>
-
{{STRUCTURE_3nva| PDB=3nva | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PYRG_SACS2 PYRG_SACS2] Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen (PubMed:21301086). Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity).[HAMAP-Rule:MF_01227]<ref>PMID:21301086</ref>
 +
== 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/nv/3nva_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=3nva ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
CTP synthase catalyzes the last committed step in de novo pyrimidine-nucleotide biosynthesis. Active CTP synthase is a tetrameric enzyme composed of a dimer of dimers. The tetramer is favoured in the presence of the substrate nucleotides ATP and UTP; when saturated with nucleotide, the tetramer completely dominates the oligomeric state of the enzyme. Furthermore, phosphorylation has been shown to regulate the oligomeric states of the enzymes from yeast and human. The crystal structure of a dimeric form of CTP synthase from Sulfolobus solfataricus has been determined at 2.5 A resolution. A comparison of the dimeric interface with the intermolecular interfaces in the tetrameric structures of Thermus thermophilus CTP synthase and Escherichia coli CTP synthase shows that the dimeric interfaces are almost identical in the three systems. Residues that are involved in the tetramerization of S. solfataricus CTP synthase according to a structural alignment with the E. coli enzyme all have large thermal parameters in the dimeric form. Furthermore, they are seen to undergo substantial movement upon tetramerization.
-
===Dimeric form of CTP synthase from Sulfolobus solfataricus===
+
Structure of the dimeric form of CTP synthase from Sulfolobus solfataricus.,Lauritsen I, Willemoes M, Jensen KF, Johansson E, Harris P Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Feb 1;67(Pt, 2):201-8. Epub 2011 Jan 21. PMID:21301086<ref>PMID:21301086</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
==About this Structure==
+
</div>
-
[[3nva]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NVA OCA].
+
<div class="pdbe-citations 3nva" style="background-color:#fffaf0;"></div>
-
[[Category: CTP synthase]]
+
== References ==
-
[[Category: Sulfolobus solfataricus]]
+
<references/>
-
[[Category: Harris, P.]]
+
__TOC__
-
[[Category: Jensen, K F.]]
+
</StructureSection>
-
[[Category: Johansson, E.]]
+
[[Category: Large Structures]]
-
[[Category: Lauritsen, I.]]
+
[[Category: Saccharolobus solfataricus]]
-
[[Category: Willemoes, M.]]
+
[[Category: Harris P]]
 +
[[Category: Jensen KF]]
 +
[[Category: Johansson E]]
 +
[[Category: Lauritsen I]]
 +
[[Category: Willemoes M]]

Current revision

Dimeric form of CTP synthase from Sulfolobus solfataricus

PDB ID 3nva

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/3nva"
Personal tools