3hqq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:52, 1 November 2023) (edit) (undo)
 
(6 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:3hqq.png|left|200px]]
 
-
<!--
+
==Crystal structure of Leishmania mexicana pyruvate kinase (LmPYK) in complex with Fructose 2,6 bisphosphate==
-
The line below this paragraph, containing "STRUCTURE_3hqq", creates the "Structure Box" on the page.
+
<StructureSection load='3hqq' size='340' side='right'caption='[[3hqq]], [[Resolution|resolution]] 5.07&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'>[[3hqq]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HQQ 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]] 5.07&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FDP:FRUCTOSE-2,6-DIPHOSPHATE'>FDP</scene></td></tr>
-
{{STRUCTURE_3hqq| PDB=3hqq | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hqq OCA], [https://pdbe.org/3hqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hqq RCSB], [https://www.ebi.ac.uk/pdbsum/3hqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hqq ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/KPYK_LEIME KPYK_LEIME]
 +
== 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/hq/3hqq_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=3hqq ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Allosteric regulation provides a rate management system for enzymes involved in many cellular processes. Ligand-controlled regulation is easily recognizable, but the underlying molecular mechanisms have remained elusive. We have obtained the first complete series of allosteric structures, in all possible ligated states, for the tetrameric enzyme, pyruvate kinase, from Leishmania mexicana. The transition between inactive T-state and active R-state is accompanied by a simple symmetrical 6 degrees rigid body rocking motion of the A- and C-domain cores in each of the four subunits. However, formation of the R-state in this way is only part of the mechanism; eight essential salt bridge locks that form across the C-C interface provide tetramer rigidity with a coupled 7-fold increase in rate. The results presented here illustrate how conformational changes coupled with effector binding correlate with loss of flexibility and increase in thermal stability providing a general mechanism for allosteric control.
-
===Crystal structure of Leishmania mexicana pyruvate kinase (LmPYK) in complex with Fructose 2,6 bisphosphate===
+
Allosteric mechanism of pyruvate kinase from Leishmania mexicana uses a rock and lock model.,Morgan HP, McNae IW, Nowicki MW, Hannaert V, Michels PA, Fothergill-Gilmore LA, Walkinshaw MD J Biol Chem. 2010 Apr 23;285(17):12892-8. Epub 2010 Feb 1. PMID:20123988<ref>PMID:20123988</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 3hqq" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_20123988}}, adds the Publication Abstract to the page
+
*[[Pyruvate kinase 3D structures|Pyruvate kinase 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 20123988 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_20123988}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
3HQQ is a 24 chains structure with sequences from [http://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HQQ OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:20123988</ref><references group="xtra"/>
+
[[Category: Leishmania mexicana]]
[[Category: Leishmania mexicana]]
-
[[Category: Pyruvate kinase]]
+
[[Category: Morgan HP]]
-
[[Category: Morgan, H P.]]
+
[[Category: Walkinshaw MD]]
-
[[Category: Walkinshaw, M D.]]
+
-
[[Category: Allosteric enzyme]]
+
-
[[Category: Glycolysis]]
+
-
[[Category: Kinase]]
+
-
[[Category: Magnesium]]
+
-
[[Category: Metal-binding]]
+
-
[[Category: Pyruvate]]
+
-
[[Category: T-state enzyme]]
+
-
[[Category: Tim barrel]]
+
-
[[Category: Transferase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 25 09:27:13 2010''
+

Current revision

Crystal structure of Leishmania mexicana pyruvate kinase (LmPYK) in complex with Fructose 2,6 bisphosphate

PDB ID 3hqq

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/3hqq"
Personal tools