2orv: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older edit
No edit summary
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2orv.gif|left|200px]]


<!--
==human Thymidine Kinase 1 in complex with TP4A==
The line below this paragraph, containing "STRUCTURE_2orv", creates the "Structure Box" on the page.
<StructureSection load='2orv' size='340' side='right'caption='[[2orv]], [[Resolution|resolution]] 2.30&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'>[[2orv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ORV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ORV 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]] 2.3&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4TA:P1-(5-ADENOSYL)P4-(5-(2-DEOXY-THYMIDYL))TETRAPHOSPHATE'>4TA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_2orv| PDB=2orv |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2orv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2orv OCA], [https://pdbe.org/2orv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2orv RCSB], [https://www.ebi.ac.uk/pdbsum/2orv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2orv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KITH_HUMAN KITH_HUMAN]
== 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/or/2orv_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=2orv ConSurf].
<div style="clear:both"></div>


'''human Thymidine Kinase 1 in complex with TP4A'''
==See Also==
 
*[[Thymidine kinase 3D structures|Thymidine kinase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Human thymidine kinase 1 (hTK1) and structurally related TKs from other organisms catalyze the initial phosphorylation step in the thymidine salvage pathway. Though ATP is known to be the preferred phosphoryl donor for TK1-like enzymes, its exact binding mode and effect on the oligomeric state has not been analyzed. Here we report the structures of hTK1 and of the Thermotoga maritima thymidine kinase (TmTK) in complex with the bisubstrate inhibitor TP4A. The TmTK-TP4A structure reveals that the adenosine moiety of ATP binds at the subunit interface of the homotetrameric enzyme and that the majority of the ATP-enzyme interactions occur between the phosphate groups and the P-loop. In the hTK1 structure the adenosine group of TP4A exhibited no electron density. This difference between hTK1 and TmTK is rationalized by a difference in the conformation of their quaternary structure. A more open conformation, as seen in the TmTK-TP4A complex structure, is required to provide space for the adenosine moiety. Our analysis supports the formation of an analogous open conformation in hTK1 upon ATP binding.
 
==About this Structure==
2ORV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ORV OCA].
 
==Reference==
Binding of ATP to TK1-like enzymes is associated with a conformational change in the quaternary structure., Segura-Pena D, Lutz S, Monnerjahn C, Konrad M, Lavie A, J Mol Biol. 2007 May 25;369(1):129-41. Epub 2007 Mar 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17407781 17407781]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Thymidine kinase]]
[[Category: Konrad M]]
[[Category: Konrad, M.]]
[[Category: Lavie A]]
[[Category: Lavie, A.]]
[[Category: Lutz S]]
[[Category: Lutz, S.]]
[[Category: Monnerjahn C]]
[[Category: Monnerjahn, C.]]
[[Category: Segura-Pena D]]
[[Category: Segura-Pena, D.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 11:32:23 2008''

Latest revision as of 12:05, 21 February 2024

human Thymidine Kinase 1 in complex with TP4Ahuman Thymidine Kinase 1 in complex with TP4A

Structural highlights

2orv is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.3Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KITH_HUMAN

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2orv, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2orv&oldid=4062178"